Alternative crystal form of monoacylglycerol lipase (MGLL)

ABSTRACT

A number of soluble engineered forms of MGLL that are suitable for high-throughput screening and protein crystallization, as well as a crystallized forms of monoacylglycerol lipase protein (MGLL) and descriptions of the X-ray diffraction patterns are disclosed. The engineered constructs of MGLL permit the expression and purification of protein suitable for crystallography or high-throughput screening and identification of ligands, which can function as active agents to MGLL. The X-ray diffraction patterns allow the three dimensional structure of MGLL to be determined at atomic resolution so that ligand binding sites on MGLL can be identified and the interactions of ligands with MGLL amino acid residues can be modeled. Models prepared using such maps permit the design of ligands which can function as active agents which include, but are not limited to, those that function as inhibitors of MGLL.

CROSS-REFERENCE TO RELATED APPLICATIONS

This application claims benefit of U.S. Provisional Patent Application Ser. No. 61/103,966 filed Oct. 9, 2008 which is incorporated herein by reference in its entirety and for all purposes.

TECHNICAL FIELD

The present invention generally pertains to the fields of molecular biology, protein purification, high-throughput screening, protein crystallization, X-ray diffraction analysis, three-dimensional structural determination, molecular modelling, and structure based rational drug design. The present invention provides a number of soluble engineered forms of MGLL that are suitable for high-throughput screening and protein crystallization, as well as crystallized forms of monoacylglycerol lipase protein (MGLL) and descriptions of the X-ray diffraction patterns.

The forms of MGLL provided by the present invention permit the expression and purification of protein suitable for high-throughput screening and crystallography. Thus forms of MGLL of the present invention have applications to the screening of MGLL to identify active agents which include, but are not limited to, those that find use as inhibitors of MGLL.

The X-ray diffraction patterns of the crystals of the present invention are of sufficient resolution so that the three-dimensional structure of MGLL can be determined at atomic resolution, ligand-binding sites on MGLL can be identified, and the interactions of ligands with amino acid residues of MGLL can be modeled. The high resolution maps provided by the present invention and the models prepared using such maps permit the design of ligands which can function as active agents. Thus, the three-dimensional structure of MGLL of the present invention has applications to the design of active agents, which include, but are not limited to, those that find use as inhibitors of MGLL.

BACKGROUND OF THE INVENTION

Various publications, which may include patents, published applications, technical articles and scholarly articles, are cited throughout the specification in parentheses, and full citations of each may be found at the end of the specification. Each of these cited publications is incorporated by reference herein, in its entirety.

Δ⁹-Tetrahydrocannabinol (THC) is the main psychoactive substance found in the cannabis plant. THC activates two distinct G protein-coupled receptors, cannabinoid 1 receptor (CB1) and cannabinoid 2 receptor (CB2) (Matsuda et al. 1990; Munro et al. 1993). CB1 is primarily expressed in the central nervous system (CNS) (Hohmann and Herkenham 1999; Farquhar-Smith et al. 2000; Rice et al. 2002; Walczak et al. 2005). CB2 expression, however, seems to be restricted to only peripheral tissues (Munro et al. 1993; Galiegue et al. 1995).

CNS mediated analgesic effects of cannabinoids have been well documented, but there is also accumulating evidence suggesting that cannabinoids can produce antinociception through peripheral mechanisms involving CB1 or CB2 (Hohmann 2002) (Malan et al. 2002). Richardson et al. demonstrated that cannabinoid antihyperalgesic effects were predominantly mediated by CB1 (Richardson et al. 1998; Richardson 2000). Hanus et al. showed that intraperitoneal injection of a CB2 selective agonist could suppress the late-phase response in the formalin test (Hanus et al. 1999). It was also shown that a CB2 selective agonist could attenuate thermal nociception and hyperalgesia (Malan et al. 2001; Malan et al. 2002; Quartilho et al. 2003) or suppress hyperalgesia evoked by intradermal administration of capsaicin (Hohmann et al. 2004). Ibrahim et al. showed that activation of CB2 with a selective CB2 agonist inhibited experimental neuropathic pain (Ibrahim et al. 2006). Taken together, the accumulating evidence clearly suggests great potential therapeutic value in targeting CB2 as a peripheral target for the treatment of pain. It should be noted that a significant advantage of this approach is that it would preclude unwanted CNS side effects caused by targeting CB1.

An arachidonic acid derivative, 2-arachidonyl glycerol (2-AG), is one of the two major and most well studied endogenous ligands for CB1 and CB2 (Gonsiorek et al. 2000). It has been shown that 2-AG acts as a potent and full-efficacy agonist of CB2 (Gonsiorek et al. 2000; Sugiura et al. 2000; Maresz et al. 2005) and that 2-AG is primarily hydrolysed by monoacylglycerol lipase (MGLL) (Dinh et al. 2002; Dinh et al. 2004; Saario et al. 2004). A non-competitive MGLL inhibitor that blocked 2-AG hydrolysis was found to enhance 2-AG levels and antinociception in stress models (Hohmann et al. 2005; Makara et al. 2005). It was also demonstrated that local administration of either 2-AG or a selective MGLL inhibitor induced a dose-dependent antinociceptive effect in an inflammatory pain model. Furthermore, local administration of the selective MGLL inhibitor in combination with 2-AG produced an additive antinociceptive effect (Guindon et al. 2007). Thus selective inhibition of MGLL may provide a novel therapeutic approach for the treatment of pain. Hitting this target, however, is inconceivable without good knowledge of the enzyme (Vandevoorde and Lambert 2005).

Lipases are lipolytic enzymes that have been differentiated from carboxylesterases by the fact that lipases have improved kinetics of hydrolysis for emulsions formed in oversaturated solutions. Carboxylesterases have been shown to have maximal activity using solutions of short-chain esters, with half-maximal activity at substrate concentrations far below the solubility limit. Exceeding the solubility limit was shown to have no effect on carboxylesterase activity. Lipases, on the other hand, were shown to have maximal activity using emulsified substrates, with half-maximal activity at substrate concentrations near the solubility limit (Chahinian et al. 2002). Early work with porcine pancreatic lipase showed that activity was low using a solution of ester substrates and abruptly increased as soon as an emulsion was formed. It was speculated that the porcine pancreatic lipase was activated by a conformational change of the enzyme as it bound to its water-insoluble substrate. The work with porcine pancreatic lipase was reviewed by Nini et al. (Nini et al. 2001).

In general, lipases share a similar α/β hydrolase fold with a catalytic Ser-His-Asp triad buried beneath a flexible cap-domain which is also referred to as a “lid” or “flap” (Brady et al. 1990; Winkler et al. 1990; Schrag et al. 1991). Although there is little conservation in the primary sequence of the cap-domain, it is generally formed of loops and one or more amphipatic helices. The cap-domains of human and dog gastric lipase are composed of intricate mixtures of 8 helices, turns, and random coils (Roussel et al. 1999; Roussel et al. 2002). In the crystal structure of human pancreatic lipase the lid adopts a helix-turn helix motif composed of two short amphipathic helices (van Tilbeurgh et al. 1992).

It has long been proposed that higher lipase activity for substrates presented as multimolecular aggregates (inter facial activation) is due to a conformational change in the cap-domain. It has also been proposed that changes from a closed to an open conformation of the lid is triggered by interaction with the substrate or lipid membrane (Brzozowski et al. 1991; van den Berg et al. 1995; van den Berg et al. 1995; Nini et al. 2001). Several other reports have also indicated that the loop covering the active site mediates lipase substrate specificity (Dugi et al. 1992; Dugi et al. 1995). It was demonstrated that movement of the helical lid results in a change in the hydrophobic-hydrophilic balance of the exterior surface of the lipase with the hydrophobic side of the lid becoming completely exposed in the active enzyme (Faustinella et al. 1992). Some lipases, such as guinea pig pancreatic lipase and bile salt-activated lipase, do not have a lid domain. Their active sites are freely accessible to solvent. As expected, based on the lack of the a cap-domain, these lipases are not activated by a lipid/water interface (Wang et al. 1997) (Carriere et al. 1997).

Although much has been learned about the structure of lipases through determination of three-dimensional structures of several microbial lipases and mammalian lipases, the three-dimensional structure of MGLL is unknown and its mechanism of action is not well understood. Furthermore, MGLL shows very little sequence similarity with other mammalian lipases and is unique among lipases in having monoglycerides as its only substrates. MGLL seems to be only distantly related to microbial proteins that include esterases, lysophospholipases, and haloperoxidases (Karlsson et al. 1997). A virtual molecular model of MGLL was built based on the crystal structure of chloroperoxidase (Saario et al. 2005; Saario et al. 2006). The model shows an alpha beta hydrolase fold with a lid domain comprised of four helices. The model, however, is only a virtual model and gives little insight into the actual mechanism of action of MGLL.

A crystal structure of MGLL would greatly facilitate the effort to discover MGLL selective inhibitors. A potential problem for crystallization experiments with MGLL is that detergents have been required to purify and stabilize MGLL in solution for both recombinant MGLL and MGLL from endogenous sources. (Tornqvist and Belfrage 1976; Somma-Delpero et al. 1995; Karlsson et al. 2000). Without detergent the purified MGLL protein was prone to aggregation. Crystallizing a detergent-solubilized protein into a structure of sufficient regularity to enable high-resolution X-ray crystallography can be problematic because well-ordered protein crystals can be difficult to obtain (U.S. Pat. No. 6,172,262B1).

The present invention provides a number of soluble engineered forms of monoacylglycerol lipase protein (MGLL) that do not require detergent for purification. The forms of MGLL provided by the present invention permit the expression and purification of protein suitable for identifying active agents in high-throughput screening and for crystallography. The present invention also provides a crystallized form of MGLL and descriptions of the X-ray diffraction patterns. Selective point mutations of hydrophobic residues in the cap-domain of MGLL generated soluble protein that did not require detergent for purification and stability. The protein displayed monomeric behaviour by gel filtration and was suitable for crystallization and high-throughput screening. In addition, selective mutation of surface lysine residues produced protein that generated crystals of improved quality. The crystal structure of MGLL was determined at atomic resolution. The forms of MGLL provide protein that can be used to identify inhibitors in high-throughput screens and the crystal structure of MGLL provides an important tool for structure-based drug design of MGLL inhibitors.

SUMMARY OF THE INVENTION

According to a first aspect of the present invention, there is provided a composition comprising a form of MGLL, or a fragment, or target structural motif or derivative thereof, wherein one or more hydrophobic residues of the cap-domain is mutated to improve solubility.

The present invention also provides a composition comprising a form of MGLL, or a fragment, or target structural motif or derivative thereof, wherein one or more hydrophobic Leucine residues of the cap-domain is mutated to improve solubility.

The present invention further provides a composition comprising a form of MGLL comprising one or more mutated hydrophobic Leucine residues of the cap-domain, wherein said one or more mutated hydrophobic Leucine residues of the cap-domain is selected from the group consisting of Leucine 162, Leucine 167, Leucine 169, Leucine 171, Leucine 174, Leucine 176, and Leucine 184, numbering based on the reference sequence for human MGLL Isoform 2 (SEQ ID NO: 1).

The present invention provides a composition comprising a form of MGLL, comprising one or more mutated hydrophobic residues of the cap-domain, wherein said one or more hydrophobic residues of the cap-domain is mutated to Serine, Glutamine, or Arginine.

In another aspect of the invention, the present invention includes a form of MGLL comprising one or more mutated hydrophobic Leucine residues of the cap-domain further comprising a Lysine mutated to an Alanine.

The present invention also includes a form of MGLL comprising one or more mutated hydrophobic Leucine residues of the cap-domain further comprising a Lysine mutated to an Alanine, wherein said Lysine residue is selected from the group consisting of Lysine 36, Lysine 160, Lysine 165, Lysine 188, Lysine 206, Lysine 226, Lysine 259 and Lysine 269, numbering based on the reference sequence for human MGLL Isoform 2.

The present invention further includes a method of identifying an agent that binds to the forms of MGLL of the present invention, comprising the steps of contacting the form of MGLL with the agent; measuring the binding of the agent to the form of MGLL; and, determining that the agent binds to the form of MGLL; thereby identifying an agent that binds to the form of MGLL.

In a preferred embodiment, the present invention includes a method of identifying an agent that binds to the forms of MGLL, wherein the form of MGLL has an amino acid sequence selected from the group consisting of SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, and SEQ ID NO: 7.

In another preferred embodiment, the present invention includes a method of identifying an agent that binds to the forms of MGLL, wherein the binding is measured by the thermal stability of the form of MGLL.

The present invention further includes a method of identifying an agent that inhibits the activity of the forms of MGLL of the present invention comprising the steps of contacting the form of MGLL with the agent; measuring the biological activity of the form of MGLL in the presence of the agent; measuring the biological activity of the form of MGLL without the agent; and, comparing the biological activity of the form of MGLL measured in the presence of the agent and without the agent; thereby identifying the agent that decreases the biological activity the biological activity of the form of MGLL, when the activity measured in the presence of the agent is less than the activity measured without the agent.

In a preferred embodiment, the present invention includes a method of identifying an agent that inhibits the activity of the forms of MGLL, wherein the form of MGLL has an amino acid sequence selected from the group consisting of SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, and SEQ ID NO: 7.

In another preferred embodiment, the present invention includes a method of identifying an agent that inhibits the activity of the forms of MGLL of the present invention, wherein the biological activity is measured with an enzyme assay.

The present invention further includes methods of producing and using three-dimensional structure information derived from the crystal structure of monoacylglycerol lipase protein (MGLL).

The present invention also includes specific crystallization conditions to obtain crystals of the inhibitor-MGLL complex. The crystals are subsequently used to obtain a 3-dimensional structure of the complex using X-ray crystallography. The obtained data is used for rational drug discovery with the aim to design compounds that are inhibitors of MGLL.

The present invention includes a crystal comprising monoacylglycerol lipase (MGLL), or a fragment, or target structural motif or derivative thereof, and a ligand, wherein the ligand is a small molecule inhibitor. In another embodiment, the crystal has a spacegroup of C222₁ or C2.

In another aspect of the invention, the present invention includes a crystal comprising a form of MGLL which comprises a peptide having at least 95% sequence identity to SEQ ID NO: 7.

In another aspect of the invention, the invention includes a computer system comprising: (a) a database containing information on the three dimensional structure of a crystal comprising MGLL, or a fragment or a target structural motif or derivative thereof, and a ligand, wherein the ligand is a small molecule inhibitor, stored on a computer readable storage medium; and, (b) a user interface to view the information.

The present invention also includes a method of evaluating the potential of an agent to associate with MGLL comprising: (a) exposing MGLL to the agent; and (b) detecting the association of said agent to MGLL amino acid residues SER48-HIS54, ARG57, TYR58, HIS77, HIS80, MET88, PHE93, PHE96, GLY120-ILE127, ILE145-VAL161, ALA163, SER176-ASN195, ASP197, ILE200, CYS201, ALA203, LEU205-VAL207, PHE209-SER218, ASP239-ASP243, TYR268-LEU275, THR279 thereby evaluating the potential of the agent.

The invention further includes a method of evaluating the potential of an agent to associate with the peptide having the sequence of SEQ ID NO: 7, comprising: (a) exposing SEQ ID NO: 7 to the agent; and (b) detecting the level of association of the agent to SEQ ID NO: 7, thereby evaluating the potential of the agent.

Further included in the present invention is a method of identifying a potential agonist or antagonist against monoacylglycerol lipase comprising: (a) employing the three dimensional structure of MGLL cocrystallized with a small molecule inhibitor to design or select said potential agonist or antagonist.

The invention comprises a method of locating the attachment site of an inhibitor to monoacylglycerol lipase, comprising: (a) obtaining X-ray diffraction data for a crystal of MGLL; (b) obtaining X-ray diffraction data for a complex of MGLL and an inhibitor; (c) subtracting the X-ray diffraction data obtained in step (a) from the X-ray diffraction data obtained in step (b) to obtain the difference in the X-ray diffraction data; (d) obtaining phases that correspond to X-ray diffraction data obtained in step (a); (e) utilizing the phases obtained in step (d) and the difference in the X-ray diffraction data obtained in step (c) to compute a difference Fourier image of the inhibitor; and, (f) locating the attachment site of the inhibitor to MGLL based on the computations obtained in step (e).

The present invention further comprises a method of obtaining a modified inhibitor comprising: (a) obtaining a crystal comprising MGLL and an inhibitor; (b) obtaining the atomic coordinates of the crystal; (c) using the atomic coordinates and one or more molecular modelling techniques to determine how to modify the interaction of the inhibitor with MGLL; and, (d) modifying the inhibitor based on the determinations obtained in step (c) to produce a modified inhibitor.

In another aspect of the invention, the invention includes an isolated protein fragment comprising a binding pocket or active site defined by structure coordinates of MGLL amino acid residues SER48-HIS54, ARG57, TYR58, HIS77, HIS80, MET88, PHE93, PHE96, GLY120-ILE127, ILE145-VAL161, ALA163, SER176-ASN195, ASP197, ILE200, CYS201, ALA203, LEU205-VAL207, PHE209-SER218, ASP239-ASP243, TYR268-LEU275, THR279.

In another aspect of the invention, the invention includes an isolated nucleic acid molecule encoding the fragment which comprises a binding pocket or active site defined by structure coordinates of MGLL amino acid residues SER48-HIS54, ARG57, TYR58, HIS77, HIS80, MET88, PHE93, PHE96, GLY120-ILE127, ILE145-VAL161, ALA163, SER176-ASN195, ASP197, ILE200, CYS201, ALA203, LEU205-VAL207, PHE209-SER218, ASP239-ASP243, TYR268-LEU275, THR279. In another aspect of the invention, the invention includes a method of screening for an agent that associates with MGLL, comprising: (a) exposing a protein molecule fragment to the agent; and (b) detecting the level of association of the agent to the fragment. In another aspect of the invention, the invention includes a kit comprising a protein molecule fragment.

The invention additionally comprises a method for the production of a crystal complex comprising a MGLL polypeptide-ligand comprising: (a) contacting the MGLL polypeptide with said ligand in a suitable solution comprising PEG MME 5K, Na Citrate and n-Octyl-Beta-D-Glucopyranoside, or a solution comprising PEG 4000 and LiCl; and b) crystallizing said resulting complex of MGLL polypeptide-ligand from said solution.

The invention further includes a method for the production of a crystal comprising MGLL and a ligand wherein the ligand is a small molecule inhibitor comprising crystallizing a peptide comprising SEQ ID NO: 7 with a potential inhibitor.

The invention includes a method for identifying a potential inhibitor of monoacylglycerol lipase comprising: a) using a three dimensional structure of MGLL as defined by atomic coordinates according to Table 6 or Table 7; b) replacing one or more MGLL amino acids selected from SER48-HIS54, ARG57, TYR58, HIS77, HIS80, MET88, PHE93, PHE96, GLY120-ILE127, ILE145-VAL161, ALA163, SER176-ASN195, ASP197, ILE200, CYS201, ALA203, LEU205-VAL207, PHE209-SER218, ASP239-ASP243, TYR268-LEU275, THR279 in said three-dimensional structure with a different amino acid to produce a modified MGLL; c) using said three-dimensional structure to design or select said potential inhibitor; d) synthesizing said potential inhibitor; and, e) contacting said potential inhibitor with said modified MGLL in the presence of a substrate to test the ability of said potential inhibitor to inhibit MGLL or said modified MGLL. Also included in the invention is an inhibitor identified by the method.

BRIEF DESCRIPTION OF THE DRAWINGS

A preferred embodiment of the present invention will now be described, by way of an example only, with reference to the accompanying drawings wherein:

FIG. 1: A. Shown is SEQ ID NO: 1, the amino acid sequence of human monoglyceride lipase isoform 2 (Karlsson et al. 2001), accession NP_(—)001003794, version NP_(—)001003794.1, GI:51242953. B. Shown is SEQ ID NO: 2, the amino acid sequence of human monoglyceride lipase isoform 1 (Wall et al. 1997), Accession NP_(—)009214, Version NP_(—)009214.1, GI:6005786. C. Shown is the sequence alignment for SEQ ID NO: 1 and SEQ ID NO: 2, which are human monoglyceride lipase isoform 2 and isoform 1, respectively. Sequence alignment was done with the online BLAST 2 SEQUENCES software (Tatusova and Madden 1999).

FIG. 2: A. Shown is the sequence alignment of human MGLL isoform 2 (SEQ ID NO: 1) and crystallized RsbQ (RsbQ, PDB 1WOM). Sequence alignment was done with the ClustalW software. Homologous residues are shown in black. Identical residues are shown in green. Position of helices and β sheets are indicated by red stars and green columns, respectively. The active site residues are highlighted in red. Leu 169 and Leu 176 are indicated by blue arrows. B. Shown is ribbon diagram representation of a homology model of human MGLL isoform 2 based on RsbQ (Pdb 1bro). Leu 169 and Leu 176 are shown in magenta. The active site residues are shown in green. C. Shown is surface representation of a homology model of human MGLL isoform 2 based on RsbQ (Pdb 1bro). Leu 169 and Leu 176 are shown in magenta. The active site residues are shown in green.

FIG. 3: A. Shown is SEQ ID NO: 3, the amino acid sequence of the construct used to express wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3). The N-terminal His tag is shown in non-capitalized text and the TEV cleavage site is shown in bold non-capitalized text with an arrow over the site of cleavage. B. Shown is SEQ ID NO: 4, the amino acid sequence of the construct used to express a form of mut-MGLL (hMGLL 1-303 L169S, L176S). The N-terminal His tag is shown in non-capitalized text, the TEV cleavage site is shown in bold non-capitalized text with an arrow over the site of cleavage, and the mutations are shown in bold non-capitalized text. C. Shown is SEQ ID NO: 5, the amino acid sequence of mut-MGLL (hMGLL 1-303 L169S, L176S) after TEV cleavage of the N-terminal His tag. The one amino acid from the TEV cleavage site that remains after TEV cleavage is shown in bold non-capitalized text and the mutations are shown in bold non-capitalized text. D. Shown is SEQ ID NO: 6, the amino acid sequence of the construct used to express a form of mut-MGLL (hMGLL 1-303 L169S, L176S, K36A). The N-terminal His tag is shown in non-capitalized text, the TEV cleavage site is shown in bold non-capitalized text with an arrow over the site of cleavage, and the mutations are shown in bold non-capitalized text. E. Shown is SEQ ID NO: 7, the amino acid sequence of mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) after TEV cleavage of the N-terminal His tag. The one amino acid from the TEV cleavage site that remains after TEV cleavage is shown in bold non-capitalized text and the mutations are shown in bold non-capitalized text.

FIG. 4: A. Shown are size exclusion elution profiles for wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) (magenta dotted lines) and TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S) (SEQ ID NO: 5) (blue solid line) purified in the absence of detergent showing 100% aggregation for wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) and 90% monomer for TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S) (SEQ ID NO: 5). B. Shown is circular dichroism structural analysis of wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) and TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S) (SEQ ID NO: 5). Far UV scans from 200 to 260 nm are shown in (i) and temperature melts from 25 to 80° C. monitored at 210 nm are shown in (ii).

FIG. 5: Shown are duplicate Michaelis-Menten curves for the hydrolysis of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S) (SEQ ID NO: 5).

FIG. 6: Shown are thermal shift data of the melting transitions for wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) (green line) and TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S) (SEQ ID NO: 5) (red line). The midpoint of the melting transition was 58° C. for wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) and 56.7° C. for TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S) (SEQ ID NO: 5).

FIG. 7: A. Shown is the structure of Compound 1. B. Shown is the structure of Compound 2. C. Shown is the structure of Compound 3.

FIG. 8: Shown is a ribbon diagram of the structure of the complex of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) and Compound 2. Color-coding is according to secondary structure (α-helices: magenta, β-sheets: yellow). The ligand (Compound 2) is drawn in ball-and-stick representation (green). The protein adopts a typical α/β hydrolase fold comprised of 8 β-sheets, with β2 being antiparallel to the other sheets. The inhibitor is located in the active site, which is capped by loops connecting α4 to α6.

FIG. 9: Shown is a surface representation of the structure for the complex of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) and Compound 2.

FIG. 10: A. Shown is a ribbon diagram of MGLL with the cap-domain (residues 145-206) colored cyan to illustrate the location of the cap-domain. B. Shown is an overlay of the ribbon diagram of MGLL (orange) onto Bromoperoxidase A1 (salmon) and Chloroperoxidase L (green); C. Shown is an overlay of the ribbon diagram of MGLL (orange) onto P. putida Esterase (grey) and Gamma Lactamase (yellow). The cap-domain was omitted for clarity to show the good alignment between the core α/β-hydrolase in all structures. D. Shown is a ribbon diagram of the MGLL cap-domain. Superposition of different cap-domains highlighting the different arrangement between MGLL and other hydrolases. E. Shown is an overlay of the ribbon diagrams of the cap-domains of Bromoperoxidase A1 (salmon) and Chloroperoxidase L (green); F. Shown is an overlay of of the ribbon diagrams of the cap-domains of P. putida Esterase (grey) and GammaLactamase (yellow).

FIG. 11: Shown is a ribbon diagram of MGLL showing the location of mutations L169S and L176S in the cap-domain that prevented protein aggregation and K36A on the loop between β2 and β4 that would make interactions with a symmetry mate if present in the wild-type protein.

Table 1: Shown is a table of the forms of MGLL of the present invention and the purification yield in mg/liter.

Table 2: Shown is a table of the kinetic constants of the various MGLL constructs using 4MC-B or C-A as substrates. Values for the 4MC-B substrate are the average of 2 or 4 separate assays. The k_(cat)/K_(M) values for the C-A substrate are the average values for the hydrolysis of five different substrate concentrations at [S]<<K_(M).

Table 3: Shown are the data collection and refinement statistics for the complex of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) and Compound 2.

Table 4: Shown are the data collection and refinement statistics for the complex of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) and Compound 3.

Table 5: Shown are the superposition statistics for selected α/β hydrolases without the cap-domain superimposed onto MGLL without the cap-domain

Table 6: Shown are the coordinates for the complex of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) and Compound 2.

Table 7: Shown are the coordinates for the complex of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) and Compound 3.

DEFINITIONS

As is generally the case in biotechnology and chemistry, the description of the present invention has required the use of a number of terms of art. Although it is not practical to do so exhaustively, definitions for some of these terms are provided here for ease of reference. Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Definitions for other terms may also appear elsewhere herein. However, the definitions provided here and elsewhere herein should always be considered in determining the intended scope and meaning of the defined terms. Although any methods and materials similar or equivalent to those described herein can be used in the practice of the present invention, the preferred methods and materials are described.

The term “comprising” means “including principally, but not necessarily solely”. Furthermore, variations of the word “comprising”, such as “comprise” and “comprises”, have correspondingly varied meanings.

As used herein, the terms “containing”, “having” and “including” are used in their open, non-limiting sense.

As used herein, “sequence” means the linear order in which monomers occur in a polymer, for example, the order of amino acids in a polypeptide or the order of nucleotides in a polynucleotide.

The terms “polypeptide”, “protein”, and “peptide” are used herein interchangeably to refer to amino acid chains in which the amino acid residues are linked by peptide bonds or modified peptide bonds. The amino acid chains can be of any length of greater than two amino acids. Unless otherwise specified, the terms “polypeptide”, “protein”, and “peptide” also encompass various modified forms thereof Such modified forms may be naturally occurring modified forms or chemically modified forms. Examples of modified forms include, but are not limited to, glycosylated forms, phosphorylated forms, myristoylated forms, palmitoylated forms, ribosylated forms, acetylated forms, ubiquitinated forms, etc. Modifications also include intra-molecular crosslinking and covalent attachment to various moieties such as lipids, flavin, biotin, polyethylene glycol or derivatives thereof, etc. In addition, modifications may also include cyclization, branching and cross-linking. Further, amino acids other than the conventional twenty amino acids encoded by the codons of genes may also be included in a polypeptide.

As used herein, a protein or nucleic acid molecule is said to be “isolated” when the protein or nucleic acid molecule is substantially separated from contaminants from the source of the protein or nucleic acid.

As used herein, the term “native protein” refers to a protein comprising an amino acid sequence identical to that of a protein isolated from its natural source or organism.

As used herein, the term “amino acids” refers to the L-isomers of the naturally occurring amino acids. The naturally occurring amino acids are glycine, alanine, valine, leucine, isoleucine, serine, methionine, threonine, phenylalanine, tyrosine, tryptophan, cysteine, proline, histidine, aspartic acid, asparagine, glutamic acid, glutamine, γ-carboxylglutamic acid, arginine, ornithine, and lysine. Unless specifically indicated, all amino acids are referred to in this application are in the L-form.

As used herein, the term “nonnatural amino acids” refers to amino acids that are not naturally found in proteins. For example, selenomethionine.

As used herein, the term “positively charged amino acid” includes any amino acids having a positively charged side chain under normal physiological conditions. Examples of positively charged naturally occurring amino acids are arginine, lysine, and histidine.

As used herein, the term “negatively charged amino acid” includes any amino acids having a negatively charged side chains under normal physiological conditions. Examples of negatively charged naturally occurring amino acids are aspartic acid and glutamic acid.

As used herein, the term “hydrophobic amino acid” includes any amino acids having an uncharged, nonpolar side chain that is relatively insoluble in water. Examples of naturally occurring hydrophobic amino acids are alanine, leucine, isoleucine, valine, proline, phenylalanine, tryptophan, and methionine.

As used herein, the term “hydrophilic amino acid” refers to any amino acids having an uncharged, polar side chain that is relatively soluble in water. Examples of naturally occurring hydrophilic amino acids are serine, threonine, tyrosine, asparagine, glutamine and cysteine.

As used herein, “nucleic acid” is defined as RNA or DNA that encodes a protein or peptide as defined herein, or is complementary to nucleic acid sequence encoding such peptides, or hybridizes to such nucleic acid and remains stably bound to it under appropriate stringency conditions. Nucleic acid sequences can be composed of natural nucleotides of the following bases: thymidine, adenine, cytosine, guanine, and uracil; abbreviated T, A, C, G, and U, respectively, and/or synthetic analogs of the natural nucleotides.

The term “oligonucleotide” or “oligo” refers to a single-stranded DNA or RNA sequence of a relatively short length, for example, less than 100 residues long. For many methods, oligonucleotides of about 16-25 nucleotides in length are useful, although longer oligonucleotides of greater than about 25 nucleotides may sometimes be utilized. Some oligonucleotides can be used as “primers” for the synthesis of complimentary nucleic acid strands. For example, DNA primers can hybridize to a complimentary nucleic acid sequence to prime the synthesis of a complimentary DNA strand in reactions using DNA polymerases. Oligonucleotides are also useful for hybridization in several methods of nucleic acid detection, for example, in Northern blotting or in situ hybridization.

“Recombinant” refers to a nucleic acid, a protein encoded by a nucleic acid, a cell, or a viral particle, that has been modified using molecular biology techniques to something other than its natural state. For example, recombinant cells can contain nucleotide sequence that is not found within the native (non-recombinant) form of the cell or can express native genes that are otherwise abnormally, under-expressed, or not expressed at all. Recombinant cells can also contain genes found in the native form of the cell wherein the genes are modified and re-introduced into the cell by artificial means. The term also encompasses cells that contain an endogenous nucleic acid that has been modified without removing the nucleic acid from the cell; such modifications include those obtained, for example, by gene replacement, and site-specific mutation.

The term “high stringency” as used herein refers to the conditions under which two nucleic acids may be hybridized, and may include, for example, the concentration of salts and/or detergents in a solution, the temperature of a solution that is used during the hybridization of the two nucleic acids and time period of the hybridization. Accordingly, the term “high stringency” as used herein refers to conditions in a solution that are conducive to hybridization of two nucleic acids only where such nucleic acids share a high degree of complementarity. The degree of complementarity may include, but not be limited to, a range of from about 90% to 100%. Thus, “high stringency” conditions may involve, but are not limited to, the use of a varying temperature and a buffer comprising various concentrations of detergents, salts, and divalent cations.

As used herein, “vector” refers to a nucleic acid molecule into which a heterologous nucleic acid can be or is inserted. Some vectors can be introduced into a host cell allowing for replication of the vector or for expression of a protein that is encoded by the vector or construct. Vectors typically have selectable markers, for example, genes that encode proteins allowing for drug resistance, origins of replication sequences, and multiple cloning sites that allow for insertion of a heterologous sequence. Vectors are typically plasmid-based and are designated by a lower case “p” followed by a combination of letters and/or numbers. Starting plasmids disclosed herein are either commercially available, publicly available on an unrestricted basis, or can be constructed from available plasmids by application of procedures known in the art. Many plasmids and other cloning and expression vectors that can be used in accordance with the present invention are well-known and readily available to those of skill in the art. Moreover, those of skill readily may construct any number of other plasmids suitable for use in the invention. The properties, construction and use of such plasmids, as well as other vectors, in the present invention will be readily apparent to those of skill from the present disclosure.

As used herein, the term “activity” refers to an activity exerted by MGLL as determined in vivo or in vitro, according to standard techniques. Examples of such activity include, but are not limited to, direct activity such as the ability to bind to a ligand or an analog thereof, enzymatic activity, or functional changes of cell physiology that result from changes in activity.

The term “high-throughput assay” or “high-throughput screening” refers to assay designs that allow easy screening of multiple samples simultaneously and/or in rapid succession, and may include the capacity for robotic manipulation. Another desired feature of high-throughput assays is an assay design that is optimized to reduce reagent usage, or minimize the number of manipulations in order to achieve the analysis desired. Examples of high-throughput assay formats include, but are not limited to, formats that utilize 96-well, 384-well, and 1536-well plates, or “lab on a chip” microchannel chips used for liquid handling experiments. It is well known by those in the art that as miniaturization of plastic molds and liquid handling devices are advanced, or as improved assay devices are designed, greater numbers of samples can be processed using the forms of the present invention. Any high-throughput screening may be utilized to test new compounds, which are identified or designed for their ability to interact with MGLL. For general information on high-throughput screening see, for example, (Devlin (editor) 1998); and (U.S. Pat. No. 5,763,263).

By the term “selecting” or “select” compounds it is intended to encompass both (a) choosing compounds from a group previously unknown to be modulators of a protein complex or interacting protein members thereof; and (b) testing compounds that are known to be capable of binding, or modulating the functions and activities of, a protein complex or interacting protein members thereof The compounds encompass numerous chemical classes, including but not limited to, small organic or inorganic compounds, natural or synthetic molecules, such as antibodies, proteins or fragments thereof, antisense nucleotides, interfering RNA (iRNA) and ribozymes, and derivatives, mimetics and analogs thereof Preferably, they are small organic compounds, i.e., those having a molecular weight of no greater than 10,000 daltons, more preferably less than 5,000 daltons.

As used herein, the term “atomic coordinates” or “structure coordinates” refers to mathematical coordinates that describe the positions of atoms in crystals of MGLL in Protein Data Bank (PDB) format, including X, Y, Z and B, for each atom. The diffraction data obtained from the crystals are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps may be used to establish the positions (i.e. coordinates X, Y and Z) of the individual atoms within the crystal. Those of skill in the art understand that a set of structure coordinates determined by X-ray crystallography is not without standard error. For the purpose of this invention, any set of structure coordinates for MGLL from any source having a root mean square deviation of non-hydrogen atoms of less than about 1.5 Å when superimposed on the non-hydrogen atom positions of the corresponding atomic coordinates of Table 6 or Table 7 are considered substantially identical or homologous. In a more preferred embodiment, any set of structure coordinates for MGLL from any source having a root mean square deviation of non-hydrogen atoms of less than about 0.75 Å. when superimposed on the non-hydrogen atom positions of the corresponding atomic coordinates of Table 6 or Table 7 are considered substantially identical or homologous.

The term “atom type” refers to the chemical element whose coordinates are measured. The abbreviations in column 3 of Table 6 and Table 7 identifies the element.

The terms “X,” “Y” and “Z” refer to the crystallographically-defined atomic position of the element measured with respect to the chosen crystallographic origin. The term “B” refers to a thermal factor that measures the mean variation of an atom's position with respect to its average position.

As used herein, the term “crystal” refers to any three-dimensional ordered array of molecules that diffracts X-rays.

As used herein, the term “carrier” in a composition refers to a diluent, adjuvant, excipient, or vehicle with which the product is mixed.

As used herein, the term “composition” refers to the combining of distinct elements or ingredients to form a whole. A composition comprises more than one element or ingredient. For the purposes of this invention, a composition will often, but not always comprise a carrier.

As used herein, “MGLL” is used to mean a protein obtained as a result of expression of monoacylglycerol lipase. Within the meaning of this term, it will be understood that human MGLL encompasses all proteins encoded by monoacylglycerol lipase, mutants thereof, conservative amino acid substitutions, alternative splice proteins thereof, and phosphorylated proteins thereof. Additionally, as used herein, it will be understood that the term “MGLL” includes monoacylglycerol lipase and homologues from other animals. As an example, MGLL includes the protein comprising SEQ ID NO: 7 and variants thereof comprising at least about 70% amino acid sequence identity to SEQ ID NO: 7, or preferably 80%, 85%, 90% and 95% sequence identity to SEQ ID NO: 7, or more preferably, at least about 95% or more sequence identity to SEQ ID NO: 7.

As used herein, the term “SAR”, an abbreviation for Structure-Activity Relationships, collectively refers to the structure-activity/structure property relationships pertaining to the relationship(s) between a compound's activity/properties and its chemical structure.

As used herein, the term “molecular structure” refers to the three dimensional arrangement of molecules of a particular compound or complex of molecules (e.g., the three dimensional structure of MGLL and ligands that interact with MGLL.

As used herein, the term “molecular modeling” refers to the use of computational methods, preferably computer assisted methods, to draw realistic models of what molecules look like and to make predictions about structure activity relationships of ligands. The methods used in molecular modeling range from molecular graphics to computational chemistry.

As used herein, the term “molecular model” refers to the three dimensional arrangement of the atoms of a molecule connected by covalent bonds or the three dimensional arrangement of the atoms of a complex comprising more than one molecule, e.g., a protein-ligand complex.

As used herein, the term “molecular graphics” refers to three dimensional (3D) representations of the molecules; for instance, a 3D representation produced using computer assisted computational methods.

As used herein, “computer readable medium” refers to any medium, which can be read and accessed directly by a computer. Such media include, but are not limited to: magnetic storage media, such as floppy discs, hard disc storage media, and magnetic tape; optical storage media such as optical discs or CD-ROM; electrical storage media such as RAM and ROM; and hybrids of these categories such as magnetic/optical storage media.

As used herein, “recorded” refers to a process for storing information on computer readable media. A skilled artisan can readily adopt any of the presently known methods for recording information on computer readable media to generate manufactures comprising an amino acid sequence and/or atomic coordinate/X-ray diffraction data information of the present invention.

As used herein, “a computer-based system” refers to the hardware means, software means, and data storage means used to analyze the sequence and/or X-ray diffraction data of the present invention. The minimum hardware means of the computer-based systems of the present invention comprises a central processing unit (CPU), input means, output means, and data storage means. A skilled artisan can readily appreciate which of the currently available computer-based systems are suitable for use in the present invention. A visualization device, such as a monitor, is optionally provided to visualize structure data.

As stated above, the computer-based systems of the present invention comprise a data storage means having stored therein sequence and/or atomic coordinate/X-ray diffraction data of the present invention and the necessary hardware means and software means for supporting and implementing an analysis means. As used herein, “data storage means” refers to memory which can store sequence or atomic coordinate/X-ray diffraction data of the present invention, or a memory access means which can access manufactures having recorded thereon the sequence or X-ray data of the present invention.

As used herein, “search means” or “analysis means” refers to one or more programs which are implemented on the computer-based system to compare a target sequence or target structural motif with the sequence or X-ray data stored within the data storage means. Search means are used to identify fragments or regions of a protein which match a particular target sequence or target motif. A variety of known algorithms are disclosed publicly and a variety of commercially available software for conducting search means are and can be used in the computer-based systems of the present invention. A skilled artisan can readily recognize that any one of the available algorithms or implementing software packages for conducting computer analyses can be adapted for use in the present computer-based systems.

As used herein, “a target structural motif”, or “target motif”, refers to any rationally selected sequence or combination of sequences in which the sequence(s) are chosen based on a three-dimensional configuration or electron density map which is formed upon the folding of the target motif There are a variety of target motifs known in the art. Protein target motifs include, but are not limited to, enzymatic active sites, inhibitor binding sites, structural subdomains, epitopes, functional domains and signal sequences. Similar motifs are known for RNA. A variety of structural formats for the input and output means can be used to input and output the information in the computer-based systems of the present invention.

As used herein, the term “computational chemistry” refers to calculations of the physical and chemical properties of the molecules.

As used herein, the term “molecular replacement” refers to a method that involves generating a preliminary model of a crystal of MGLL whose coordinates are unknown, by orienting and positioning the said atomic coordinates described in the present invention so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. (Rossmann 1972)

As used herein, the term “homolog” refers to the MGLL protein molecule or the nucleic acid molecule which encodes the protein, or a functional domain from said protein from a first source having at least about 70% or 75% sequence identity, or at least about 80% sequence identity, or more preferably at least about 85% sequence identity, or even more preferably at least about 90% sequence identity, and most preferably at least about 95%, 97% or 99% amino acid or nucleotide sequence identity, with the protein, encoding nucleic acid molecule or any functional domain thereof, from a second source. The second source may be a version of the molecule from the first source that has been genetically altered by any available means to change the primary amino acid or nucleotide sequence or may be from the same or a different species than that of the first source.

As used herein, the term “active site” refers to regions on MGLL or a structural motif of MGLL that are directly involved in the function or activity of human MGLL.

As used herein, the terms “binding site” or “binding pocket” refer to a region of human MGLL or a molecular complex comprising MGLL that, as a result of the primary amino acid sequence of human MGLL and/or its three-dimensional shape, favourably associates with another chemical entity or compound including ligands, cofactors, or inhibitors. For the purpose of this invention, any active site, binding site or binding pocket defined by a set of structure coordinates for MGLL or for a homolog of MGLL from any source having a root mean square deviation of non-hydrogen atoms of less than about 1.5 Å. when superimposed on the non-hydrogen atom positions of the corresponding atomic coordinates of Table 6 or Table 7 are considered substantially identical or homologous. In a more preferred embodiment, any set of structure coordinates for MGLL or a homolog of MGLL from any source having a root mean square deviation of non-hydrogen atoms of less than about 0.75 Å. when superimposed on the non-hydrogen atom positions of the corresponding atomic coordinates of Table 6 or Table 7 are considered substantially identical or homologous.

The term “root mean square deviation” means the square root of the arithmetic mean of the squares of the deviations from the mean.

As used herein, the term “hydrogen bond” refers to two hydrophilic atoms (either O or N), which share a hydrogen that is covalently bonded to only one atom, while interacting with the other.

As used herein, the term “hydrophobic interaction” refers to interactions made by two hydrophobic residues or atoms (such as C).

As used herein, the term “conjugated system” refers to more than two double bonds adjacent to each other, in which electrons are completely delocalized with the entire system. This also includes aromatic residues.

As used herein, the term “aromatic residue” refers to amino acids with side chains having a delocalized conjugated system. Examples of aromatic residues are phenylalanine, tryptophan, and tyrosine.

As used herein, the phrase “inhibiting the binding” refers to preventing or reducing the direct or indirect association of one or more molecules, peptides, proteins, enzymes, or receptors, or preventing or reducing the normal activity of one or more molecules, peptides, proteins, enzymes or receptors, e.g., preventing or reducing the direct or indirect association with human MGLL.

As used herein, the term “competitive inhibitor” refers to inhibitors that bind to human MGLL, thus directly competing with a substrate or ligand. Competitive inhibition may, in some instances, be reversed completely by increasing the substrate or ligand concentration.

As used herein, the term “uncompetitive inhibitor” refers to one that inhibits the functional activity of human MGLL by binding to a different site than does its substrate(s). As used herein, the term “non-competitive inhibitor” refers to one that can bind to either the free or bound form of MGLL. Those of skill in the art may identify inhibitors as competitive, uncompetitive, or non-competitive by computer fitting enzyme kinetic data using standard methods. See, for example, (Segel 1975)

As used herein, the term “R or S-isomer” refers to two possible stereoisomers of a chiral carbon according to the Cahn-Ingold-Prelog system adopted by International Union of Pure and Applied Chemistry (IUPAC). Each group attached to the chiral carbon is first assigned to a preference or priority a, b, c, or d on the basis of the atomic number of the atom that is directly attached to the chiral carbon. The group with the highest atomic number is given the highest preference a, the group with next highest atomic number is given the next highest preference b, and so on. The group with the lowest preference (d) is then directed away from the viewer. If the trace of a path from a to b to c is counter clockwise, the isomer is designated (S); in the opposite direction, clockwise, the isomer is designated (R).

As used herein, the term “stereoisomers” is a general term for all isomers of individual molecules that differ only in the orientation of their atoms in space. It includes enantiomers and isomers of compounds with more than one chiral center that are not mirror images of one another (diastereomers).

As used herein, the term “chiral center” refers to a carbon atom to which four different groups are attached.

As used herein, the term “enantiomer” or “enantiomeric” refers to a molecule that is nonsuperimposable on its mirror image and hence optically active wherein the enantiomer rotates the plane of polarized light in one direction and its mirror image rotates the plane of polarized light in the opposite direction.

As used herein, the term “racemic” refers to a mixture of equal parts of enantiomers and which is optically active.

As used herein, the term “resolution” refers to the separation or concentration or depletion of one of the two enantiomeric forms of a molecule. In the context of this application. The term “resolution” also refers to the amount of detail, which can be resolved by the diffraction experiment. Or in other terms, since the inherent disorder of a protein crystal diffraction pattern fades away at some diffraction angle theta_(max), the corresponding distance d_(min) of the reciprocal lattices is determined by Bragg's law. In practice in protein crystallography it is usual to quote the nominal resolution of a protein electron density in terms of d_(min), the minimum lattice distance to which data is included in the calculation of the map.

As used herein, the term “ligand” refers to any molecule, or chemical entity, which binds with or to MGLL, a subunit of MGLL, a domain of MGLL, a target structural motif of MGLL, or a fragment of MGLL. Thus, ligands include, but are not limited to, small molecule inhibitors, for example.

As used herein, the term “small molecule inhibitor” refers to compounds useful in the present invention having measurable MGLL inhibiting activity. In addition to small organic molecules, peptides, antibodies, cyclic peptides and peptidomimetics are contemplated as being useful in the disclosed methods. Preferred inhibitors are small molecules, preferably less than 10,000 daltons, and more preferably less than 5,000 daltons.

As used herein the terms “bind”, “binding”, “bond”, or “bonded” when used in reference to the association of atoms, molecules, or chemical groups, refer to any physical contact or association of two or more atoms, molecules, or chemical groups.

As used herein, the terms “covalent bond” or “valence bond” refer to a chemical bond between two atoms in a molecule created by the sharing of electrons, usually in pairs, by the bonded atoms.

As used herein, “noncovalent bond” refers to an interaction between atoms and/or molecules that does not involve the formation of a covalent bond between them.

DETAILED DESCRIPTION OF ILLUSTRATIVE EMBODIMENTS

It is to be understood at the outset, that the figures and examples provided herein are to exemplify, and not to limit the invention and its various embodiments.

The present invention includes a crystal comprising monoacylglycerol lipase (MGLL), or a fragment, or target structural motif or derivative thereof, and a ligand, wherein the ligand is a small molecule inhibitor. In one embodiment, the fragment or derivative thereof is a peptide comprising SEQ ID NO: 7

In another embodiment, the crystal has a spacegroup of C222₁ or C2. In a different embodiment, the crystal effectively diffracts X-rays for determination of atomic coordinates to a resolution of at least about 3.2 Å. In a preferred embodiment, the ligand is in crystalline form. In a highly preferred embodiment, the ligand is the structure depicted in FIG. 7A, FIG. 7B, FIG. 7C, or derivatives thereof.

The present invention also includes a crystal comprising MGLL, which comprises a peptide having at least 95% sequence identity to SEQ ID NO. 6. In a preferred embodiment, the crystal comprising SEQ ID NO: 7 comprises an atomic structure characterized by the coordinates of Table 6 or Table 7. In another preferred embodiment, the crystal comprises a unit cell selected from the group consisting of: a cell having dimensions of a=93.95, b=128.45, c=60.6 or a cell having dimensions of a=128.6, b=72.0, c=65.2

In another aspect of the invention, the invention includes a computer system comprising: (a) a database containing information on the three dimensional structure of a crystal comprising MGLL, or a fragment or a target structural motif or derivative thereof, and a ligand, wherein the ligand is a small molecule inhibitor, stored on a computer readable storage medium; and, (b) a user interface to view the information. In one embodiment, the information comprises diffraction data obtained from a crystal comprising SEQ ID NO: 7.

In another embodiment, the information comprises an electron density map of a crystal form comprising SEQ ID NO: 7. In a different embodiment, the information comprises the structure coordinates of Table 6, Table 7, or homologous structure coordinates comprising a root mean square deviation of non-hydrogen atoms of less than about 1.5 Å when superimposed on the non-hydrogen atom positions of the corresponding atomic coordinates of Table 6 or Table 7. In a preferred embodiment, the information comprises structure coordinates comprising a root mean square deviation of non-hydrogen atoms of less than about 0.75 Å when superimposed on the non-hydrogen atom positions of the corresponding atomic coordinates of Table 6 or Table 7. In a highly preferred embodiment, the information comprises the structure coordinates for amino acids SER48-HIS54, ARG57, TYR58, HIS77, HIS80, MET88, PHE93, PHE96, GLY120-ILE127, ILE145-VAL161, ALA163, SER176-ASN195, ASP197, ILE200, CYS201, ALA203, LEU205-VAL207, PHE209-SER218, ASP239-ASP243, TYR268-LEU275, THR279 according to Table 6, Table 7, or similar structure coordinates for said amino acids comprising a root mean square deviation of non-hydrogen atoms of less than about 1.5 Å to 0.75 Å when superimposed on the non-hydrogen atom positions of the corresponding atomic coordinates of Table 6 or Table 7.

The present invention also includes a method of evaluating the potential of an agent to associate with MGLL comprising: (a) exposing MGLL to the agent; and (b) detecting the association of said agent to MGLL amino acid residues SER48-HIS54, ARG57, TYR58, HIS77, HIS80, MET88, PHE93, PHE96, GLY120-ILE127, ILE145-VAL161, ALA163, SER176-ASN195, ASP197, ILE200, CYS201, ALA203, LEU205-VAL207, PHE209-SER218, ASP239-ASP243, TYR268-LEU275, THR279 thereby evaluating the potential. In one embodiment of the invention, the agent is a virtual compound. In another embodiment of the invention, step (a) comprises comparing the atomic structure of the compound to the three dimensional structure of MGLL. In a different embodiment, the comparing of step (a) comprises employing a computational means to perform a fitting operation between the compound and at least one binding site of MGLL. In a preferred embodiment, the binding site is defined by structure coordinates for amino acids SER48-HIS54, ARG57, TYR58, HIS77, HIS80, MET88, PHE93, PHE96, GLY120-ILE127, ILE145-VAL161, ALA163, SER176-ASN195, ASP197, ILE200, CYS201, ALA203, LEU205-VAL207, PHE209-SER218, ASP239-ASP243, TYR268-LEU275, THR279 according to Table 6, Table 7, or similar structure coordinates for said amino acids comprising a root mean square deviation of non-hydrogen atoms of less than about 1.5 Å when superimposed on the non-hydrogen atom positions of the corresponding atomic coordinates of Table 6 or Table 7. In a highly preferred embodiment, step (a) comprise exposing the agent to crystalline SEQ ID NO: 7 and the detecting of step (b) comprises determining the three dimensional structure of the agent-SEQ ID NO: 7 complex.

The present invention includes a method of identifying a potential agonist or antagonist against MGLL comprising: (a) employing the three dimensional structure of MGLL cocrystallized with a small molecule inhibitor to design or select said potential agonist or antagonist. In one embodiment, the three dimensional structure corresponds to the atomic structure characterized by the coordinates of Table 6, Table 7, or similar structure coordinates comprising a root mean square deviation of non-hydrogen atoms of less than about 1.5 Å when superimposed on the non-hydrogen atom positions of the corresponding atomic coordinates of Table 6 or Table 7. In a different embodiment, the method further comprises the steps of: (b) synthesizing the potential agonist or antagonist; and (c) contacting the potential agonist or antagonist with MGLL.

The instant invention comprises a method of locating the attachment site of an inhibitor to MGLL, comprising: (a) obtaining X-ray diffraction data for a crystal of MGLL; (b) obtaining X-ray diffraction data for a complex of MGLL and an inhibitor; (c) subtracting the X-ray diffraction data obtained in step (a) from the X-ray diffraction data obtained in step (b) to obtain the difference in the X-ray diffraction data; (d) obtaining phases that correspond to X-ray diffraction data obtained in step (a); (e) utilizing the phases obtained in step (d) and the difference in the X-ray diffraction data obtained in step (c) to compute a difference Fourier image of the inhibitor; and, (f) locating the attachment site of the inhibitor to MGLL based on the computations obtained in step (e).

The present invention further comprises a method of obtaining a modified inhibitor comprising: (a) obtaining a crystal comprising MGLL and an inhibitor; (b) obtaining the atomic coordinates of the crystal; (c) using the atomic coordinates and one or more molecular modeling techniques to determine how to modify the interaction of the inhibitor with MGLL; and, (d) modifying the inhibitor based on the determinations obtained in step (c) to produce a modified inhibitor. In one embodiment, the crystal comprises a peptide having a sequence comprising SEQ ID NO: 7. In a different embodiment, the one or more molecular modeling techniques are selected from the group consisting of graphic molecular modeling and computational chemistry. In a preferred embodiment, step (a) comprises detecting the interaction of the inhibitor to MGLL amino acid residues SER48-HIS54, ARG57, TYR58, HIS77, HIS80, MET88, PHE93, PHE96, GLY120-ILE127, ILE145-VAL161, ALA163, SER176-ASN195, ASP197, ILE200, CYS201, ALA203, LEU205-VAL207, PHE209-SER218, ASP239-ASP243, TYR268-LEU275, THR279. In another embodiment of the invention, the invention includes an MGLL inhibitor identified by this method.

In another aspect of the invention, the invention includes an isolated protein fragment comprising a binding pocket or active site defined by structure coordinates of MGLL amino acid residues SER48-HIS54, ARG57, TYR58, HIS77, HIS80, MET88, PHE93, PHE96, GLY120-ILE127, ILE145-VAL161, ALA163, SER176-ASN195, ASP197, ILE200, CYS201, ALA203, LEU205-VAL207, PHE209-SER218, ASP239-ASP243, TYR268-LEU275, THR279. In one embodiment, the isolated fragment is linked to a solid support.

In another aspect of the invention, the invention includes an isolated nucleic acid molecule encoding the fragment, which comprises a binding pocket or active site defined by structure coordinates of MGLL. In one embodiment, a vector comprises the nucleic acid molecule. In another embodiment, a host cell comprises the vector. In yet another aspect of the invention, the invention includes a method of producing a protein fragment, comprising culturing the host cell under conditions in which the fragment is expressed. In another aspect of the invention, the invention includes a method of screening for an agent that associates with MGLL, comprising: (a) exposing a protein molecule fragment to the agent; and (b) detecting the level of association of the agent to the fragment. In another aspect of the invention, the invention includes a kit comprising a protein molecule fragment.

In another aspect of the invention, the invention includes a method for the production of a crystal complex comprising an MGLL polypeptide-ligand comprising: (a) contacting the MGLL polypeptide with said ligand in a suitable solution comprising PEG MME, Na Citrate, and n-Octyl-Beta-D-Glucopyranoside, or a solution comprising PEG and LiCl; and, b) crystallizing said resulting complex of MGLL polypeptide-ligand from said solution. In one embodiment, the MGLL polypeptide is a polypeptide SEQ ID NO: 7. In another embodiment, PEG MME has an average molecular weight range from 2000 to 10000, wherein said PEG MME is present in solution at a range from about 1% to about 5% and said n-Octyl-Beta-D-Glucopyranoside is present in solution at a range of from about 0.2% to 2%. In a preferred embodiment, PEG MME has an average molecular weight of about 5000 and is present in solution at about 2.4% and said n-Octyl-Beta-D-Glucopyranoside is present in solution at about 0.6%. In another embodiment, said solution with PEG and LiCl, comprises PEG with an average molecular weight range from 1000 to 10000, wherein said PEG is present in solution at a range from about 5% to about 30% and said LiCl is present in solution at a range of from about 30 mM to 200 mM. In a preferred embodiment, PEG has an average molecular weight of about 4000 and is present in solution at about 7.5% and said LiCl is present in solution at of about 60 mM

The invention further includes a method for the production of a crystal comprising MGLL and a ligand wherein the ligand is a small molecule inhibitor comprising crystallizing a peptide comprising SEQ ID NO: 7 with a potential inhibitor.

The invention includes a method for identifying a potential inhibitor of MGLL comprising: a) using a three dimensional structure of MGLL as defined by atomic coordinates according to Table 6 or Table 7; b) replacing one or more MGLL amino acids selected from SER48-HIS54, ARG57, TYR58, HIS77, HIS80, MET88, PHE93, PHE96, GLY120-ILE127, ILE145-VAL161, ALA163, SER176-ASN195, ASP197, ILE200, CYS201, ALA203, LEU205-VAL207, PHE209-SER218, ASP239-ASP243, TYR268-LEU275, THR279 in said three-dimensional structure with a different amino acid to produce a modified MGLL; c) using said three-dimensional structure to design or select said potential inhibitor; d) synthesizing said potential inhibitor; and, e) contacting said potential inhibitor with said modified MGLL in the presence of a substrate to test the ability of said potential inhibitor to inhibit MGLL or said modified MGLL. In another embodiment, the potential inhibitor is selected from a database. In a preferred embodiment, the potential inhibitor is designed de novo. In another preferred embodiment, the potential inhibitor is designed from a known inhibitor. In a highly preferred embodiment, the step of employing said three-dimensional structure to design or select said potential inhibitor comprises the steps of: a) identifying chemical entities or fragments capable of associating with modified MGLL; and b) assembling the identified chemical entities or fragments into a single molecule to provide the structure of said potential inhibitor. In one embodiment, the potential inhibitor is a competitive inhibitor of SEQ ID NO: 7. In a different embodiment, the potential inhibitor is a non-competitive or uncompetitive inhibitor of SEQ ID NO: 7. In yet another embodiment, an inhibitor is identified by the method.

Engineered Forms and Fragments

Engineered forms of MGLL or fragments thereof, for instance engineered forms or fragments comprising active sites defined by two or more amino acids selected from the group consisting of: SER48-HIS54, ARG57, TYR58, HIS77, HIS80, MET88, PHE93, PHE96, GLY120-ILE127, ILE145-VAL161, ALA163, SER176-ASN195, ASP197, ILE200, CYS201, ALA203, LEU205-VAL207, PHE209-SER218, ASP239-ASP243, TYR268-LEU275, THR279 may be prepared by any available means including synthetic or recombinant means. Such fragments may then be used in the assays as described herein, for example, but not limited to, high-throughput assays to detect interactions between prospective agents and the active site within the fragment.

For recombinant expression or production of the forms or fragments of the invention, nucleic acid molecules encoding the form or fragment may be prepared. Nucleic acid molecules encoding engineered forms or fragments of the invention may differ in sequence because of the degeneracy in the genetic code or may differ in sequence as they encode proteins or protein fragments that differ in amino acid sequence. Homology or sequence identity between two or more such nucleic acid molecules is determined by BLAST (Basic Local Alignment Search Tool) analysis using the algorithm employed by the programs blastp, blastn, blastx, tblastn and tblastx (Karlin and Altschul 1990) and (Altschul 1993), fully incorporated by reference, which are tailored for sequence similarity searching.

The approach used by the BLAST program is to first consider similar segments between a query sequence and a database sequence, then to evaluate the statistical significance of all matches that are identified and finally to summarize only those matches which satisfy a preselected threshold of significance. For a discussion of basic issues in similarity searching of sequence databases, see (Altschul et al. 1994) which is fully incorporated by reference. The search parameters for histogram, descriptions, alignments, expect (i.e., the statistical significance threshold for reporting matches against database sequences), cutoff, matrix and filter are at the default settings. For a discussion of default scoring matrix used by blastp, blastx, tblastn, and tblastx, see (Henikoff 1992).

The encoding nucleic acid molecules of the present invention or fragments thereof (i.e., synthetic oligonucleotides) and those that are used as probes or specific primers for polymerase chain reaction (PCR) or to synthesize gene sequences encoding proteins of the invention can easily be synthesized by chemical techniques, for example, the phosphotriester method of (Matteucci and Caruthers 1981) or using automated synthesis methods. In addition, larger DNA segments can readily be prepared by well-known methods, such as synthesis of a group of oligonucleotides that define various modular segments of the gene, followed by ligation of oligonucleotides to build the complete modified gene.

The encoding nucleic acid molecules of the present invention may further be modified so as to contain a detectable label for diagnostic and probe purposes. A variety of such labels are known in the art and can readily be employed with the encoding molecules herein described. Suitable labels include, but are not limited to, biotin, radiolabeled nucleotides and the like. A skilled artisan can employ any of the art-known labels to obtain a labeled encoding nucleic acid molecule.

The present invention further provides recombinant DNA molecules (rDNA) that contain a coding sequence for a protein or protein fragment as described herein. As used herein, an rDNA molecule is a DNA molecule that has been subjected to molecular manipulation. Methods for generating rDNA molecules are well known in the art, for example, see (Sambrook et al. 1989). In the preferred rDNA molecules, a coding DNA sequence is operably linked to expression control sequences and/or vector sequences.

The choice of vector and expression control sequences to which one of the protein encoding sequences of the present invention is operably linked depends directly, as is well known in the art, on the functional properties desired (e.g., protein expression, and the host cell to be transformed). A vector of the present invention may be capable of directing the replication or insertion into the host chromosome, and preferably also expression, of the structural gene included in the rDNA molecule.

Expression control elements that are used for regulating the expression of an operably linked protein encoding sequence are known in the art and include, but are not limited to, inducible promoters, constitutive promoters, secretion signals, and other regulatory elements. Preferably, the inducible promoter is readily controlled, such as being responsive to a nutrient in the host cell's medium.

The present invention further provides host cells transformed with a nucleic acid molecule that encodes a protein or protein fragment of the present invention. The host cell can be either prokaryotic or eukaryotic. Eukaryotic cells useful for expression of a protein of the invention are not limited, so long as the cell line is compatible with cell culture methods and compatible with the propagation of the expression vector and expression of the gene product. Preferred eukaryotic host cells include, but are not limited to, insect, yeast, and mammalian cells. Preferred eukaryotic host cells include Spodoptera frugiperda (Sf9 or Sf21) insect cells.

Transformed host cells of the invention may be cultured under conditions that allow the production of the recombinant protein. Optionally the recombinant protein is isolated from the medium or from the cells; recovery and purification of the protein may not be necessary in some instances where some impurities may be tolerated.

Kits may also be prepared with any of the above described nucleic acid molecules, proteins, protein fragments, vector and/or host cells optionally packaged with the reagents needed for a specific assay, such as those described above. In such kits, the protein, protein fragments, or other reagents may be attached to a solid support, such as glass or plastic beads.

High-Throughput Assays

Compound identification methods can be performed using conventional laboratory assay formats or in high-throughput assays, including, but not limited to, those described below.

Immunoassays are a group of techniques used for the measurement of specific biochemical substances, commonly at low concentrations in complex mixtures such as biological fluids. The assays depend upon suitably prepared and selected antibodies with specificity and high affinity for their complementary antigens. A substance to be measured must, of necessity, be antigenic, either an immunogenic macromolecule or a haptenic small molecule. To each sample a known limited amount of specific antibody is added and the fraction of the antigen combining with it, often expressed as the bound:free ratio, is estimated by quantifying the signal from the antibody. Quantification can be achieved with a number of readily identifiable labeles and used for various types of assays, including, but not limited to, radioisotopes for radioimmunoassays (RIA), fluorescent molecules for fluoroimmunoassays (FIA), stable free radicals for spin immunoassays, chemiluminescent molecules for chemiluminescent immunoassays (CLIA), colloidal gold particles for immunogold assays, and enzymes for enzyme-linked immunosorbent assays (ELISA).

A common immunoassay format is the ELISA, which avoids the hazards of radiochemicals and the expense of fluorescence detection systems. Instead, an ELISA is a form of quantitative immunoassay based on the use of antibodies (or antigens) that may be linked to an insoluble carrier surface, which is then used to “capture” the relevant antigen (or antibody) the test solution. The antigen-antibody complex is then detected by measuring the activity of an appropriate enzyme that can be covalently attached to the capture antigen (or antibody) or to a subsequent “detection” antibody (or antigen). For more information on ELISA techniques, see, for example, (Crowther 1995); (Kemeny (editor) and Challacombe (editor) 1988), (Kemeny 1991), and (Ishikawa 1999).

Colorimetric assays for enzymes are methods of quantitative chemical analysis in which the concentration or amount of a compound is determined by comparing the color produced by the reaction of a reagent with both standard and test amounts of the compound, often using a colorimeter. A colorimeter is a device for measuring color intensity or differences in color intensity, either visually or photoelectrically. Standard colorimetric assays of beta-galactosidase enzymatic activity are well known to those skilled in the art, see for example, (Norton and Coffin 1985). A colorimetric assay can be performed on whole cell lysates using O-nitrophenyl-beta-D-galacto-pyranoside (ONPG, Sigma) as the substrate in a standard colorimetric beta-galactosidase assay (Sambrook et al. 1989). Automated colorimetric assays are also available for the detection of beta-galactosidase activity, as described in (U.S. Pat. No. 5,733,720).

Enzymatic substrates that become fluorescent after being acted upon by an enzyme generally are well known. Such fluorescent substrates typically have two components that are bound to one another through, for example, a covalent chemical bond. One component is a fluorescent molecule that is capable of fluorescing by first accepting light energy and then emitting light energy. The other component is an entity that prevents the fluorescent molecule from accepting or emitting light energy when the two components are covalently bound to one another. In the presence of an appropriate enzyme, the enzyme cleaves the covalent bond between the two components and separates one component from the other to permit the fluorescent molecule to accept and emit light energy. In other words, the enzyme frees the fluorescent molecule and allows it to fluoresce. Ideally, fluorescent substrates should be soluble and stable in aqueous buffers, should have a high affinity for the enzymes that act upon them, and should yield a strong signal upon enzymatic action (U.S. Pat. No. 5,998,593A).

Detecting fluorescence emitted from the fluorescent component of a fluorescent enzyme substrate is typically achieved in two steps. In particular, the fluorescent molecule is first excited with light energy and subsequently the fluorescence emitted from the fluorescent component is then detected. Generally, fluorescent molecules can be excited with light energy from, for example, a laser or another suitable light source. Fluorescence is detected with a device designed to detect light energy of a wavelength that is emitted by the fluorescent molecule. Such excitation and emission detection systems generally are designed to operate at particular wavelength ranges (U.S. Pat. No. 5,998,593A).

Thermofluor® assays detect small changes in the intrinsic melting temperature of proteins based on binding of ligands. Compounds that interact preferentially with the native form of the protein will increase the T_(m), the temperature at which half of the protein is unfolded (Pantoliano et al. 2001). The technique monitors changes in the fluorescent intensity of dyes such as 1-anilinonaphthalene-8-sulfonic acid (1,8-ANS). The fluorescent dyes are quenched in aqueous environments but increase in fluorescence on binding to the hydrophobic core of denatured proteins.

Modeling the Three-Dimensional Structure of MGLL

The atomic coordinate data provided in Table 6 or Table 7, or the coordinate data derived from homologous proteins may be used to build a three-dimensional model of MGLL. Any available computational methods may be used to build the three dimensional model. As a starting point, the X-ray diffraction pattern obtained from the assemblage of the molecules or atoms in a crystalline version of MGLL or an MGLL homolog can be used to build an electron density map using tools well known to those skilled in the art of crystallography and X-ray diffraction techniques. Additional phase information extracted either from the diffraction data and available in the published literature and/or from supplementing experiments may then be used to complete the reconstruction.

For basic concepts and procedures of collecting, analyzing, and utilizing X-ray diffraction data for the construction of electron densities see, for example, (Campbell 1984), (Cantor and Schimmel 1980), (Brunger 1993), (Woolfson 1997), (Drenth 1999), (Tsirelson and Ozerov 1996), and (U.S. Pat. No. 5,942,428A); (U.S. Pat. No. 6,037,117A); (U.S. Pat. No. 5,200,910A); and (U.S. Pat. No. 5,365,456A), each of which is herein specifically incorporated by reference in their entirety.

For basic information on molecular modeling, see, for example, (Schlecht 1998); (Gans et al. 1996); (Cohen (editor) 1996); and (Smith 1996). U.S. patents which provide detailed information on molecular modeling include (U.S. Pat. No. 4,906,122A; U.S. Pat. No. 5,030,103A; U.S. Pat. No. 5,583,973A; U.S. Pat. No. 5,612,894A; U.S. Pat. No. 5,994,503A; U.S. Pat. No. 6,071,700A; U.S. Pat. No. 6,075,014A; U.S. Pat. No. 6,075,123A; U.S. Pat. No. 6,080,576A; U.S. Pat. No. 6,093,573A), each of which are incorporated by reference herein in their entirety.

Methods of Using the Atomic Coordinates to Identify and Design Ligands of Interest

The atomic coordinates of the invention, such as those described in Table 6 and Table 7, or coordinates substantially identical to or homologous to those of Table 6 or Table 7 may be used with any available methods to prepare three dimensional models of MGLL as well as to identify and design MGLL ligands, inhibitors or antagonists or agonist molecules. Such a method provides the amino acid sequence and/or X-ray diffraction data in a form which allows a skilled artisan to analyze and molecular model the three-dimensional structure of MGLL or related molecules, including a subdomain thereof.

For instance, three-dimensional modeling may be performed using the experimentally determined coordinates derived from X-ray diffraction patterns, such as those in Table 6 or Table 7, for example, wherein such modeling includes, but is not limited to, drawing pictures of the actual structures, building physical models of the actual structures, and determining the structures of related subunits and MGLL/ligand and MGLL subunit/ligand complexes using the coordinates. Such molecular modeling can utilize known X-ray diffraction molecular modeling algorithms or molecular modeling software to generate atomic coordinates corresponding to the three-dimensional structure of MGLL.

As described above, molecular modeling involves the use of computational methods, preferably computer assisted methods, to build realistic models of molecules that are identifiably related in sequence to the known crystal structure. It also involves modeling new small molecule inhibitors bound to MGLL starting with the structures of MGLL and or MGLL complexed with known ligands or inhibitors. The methods utilized in ligand modeling range from molecular graphics (i.e., 3D representations) to computational chemistry (i.e., calculations of the physical and chemical properties) to make predictions about the binding of ligands or activities of ligands; to design new ligands; and to predict novel molecules, including ligands such as drugs, for chemical synthesis, collectively referred to as rational drug design.

One approach to rational drug design is to search for known molecular structures that might bind to an active site. Using molecular modeling, rational drug design programs can look at a range of different molecular structures of drugs that may fit into the active site of an enzyme, and by moving them in a three-dimensional environment it can be decided which structures actually fit the site well.

An alternative but related rational drug design approach starts with the known structure of a complex with a small molecule ligand and models modifications of that small molecule in an effort to make additional favourable interactions with MGLL.

The present invention includes the use of molecular and computer modeling techniques to design and select and design ligands, such as small molecule agonists or antagonists or other therapeutic agents that interact with MGLL. For example, the invention as herein described includes the design of ligands that act as competitive inhibitors of at least one MGLL function by binding to all, or a portion of, the active sites or other regions of MGLL.

This invention also includes the design of compounds that act as uncompetitive inhibitors of at least one function of MGLL. These inhibitors may bind to all, or a portion of, the active sites or other regions of MGLL already bound to its substrate and may be more potent and less non-specific than competitive inhibitors that compete for MGLL active sites. Similarly, non-competitive inhibitors that bind to and inhibit at least one function of MGLL whether or not it is bound to another chemical entity may be designed using the atomic coordinates of MGLL or complexes comprising MGLL of this invention.

The atomic coordinates of the present invention also provide the needed information to probe a crystal of MGLL with molecules composed of a variety of different chemical features to determine optimal sites for interaction between candidate inhibitors and/or activators and MGLL. For example, high resolution X-ray diffraction data collected from crystals saturated with solvent allows the determination of where each type of solvent molecule sticks. Small molecules that bind to those sites can then be designed and synthesized and tested for their inhibitory activity (Travis 1993).

The present invention also includes methods for computationally screening small molecule databases and libraries for chemical entities, agents, ligands, or compounds that can bind in whole, or in part, to MGLL. In this screening, the quality of fit of such entities or compounds to the binding site or sites may be judged either by shape complementarity or by estimated interaction energy (Meng et al. 1992).

The design of compounds that bind to, promote or inhibit the functional activity of MGLL according to this invention generally involves consideration of two factors. First, the compound must be capable of physically and structurally associating with MGLL. Non-covalent molecular interactions important in the association of MGLL with the compound include hydrogen bonding, van der Waals and hydrophobic interactions. Second, the compound must be able to assume a conformation that allows it to associate with MGLL. Although certain portions of the compound may not directly participate in the association with MGLL, those portions may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on binding affinities, therapeutic efficacy, drug-like qualities and potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity or compound in relation to all or a portion of the active site or other region of MGLL, or the spacing between functional groups of a compound comprising several chemical entities that directly interact with MGLL.

The potential, predicted, inhibitory agonist, antagonist or binding effect of a ligand or other compound on MGLL may be analyzed prior to its actual synthesis and testing by the use of computer modeling techniques. If the theoretical structure of the given compound suggests insufficient interaction and association between it and MGLL, synthesis and testing of the compound may be obviated. However, if computer modeling indicates a strong interaction, the molecule may then be synthesized and tested for its ability to interact with MGLL. In this manner, synthesis of inoperative compounds may be avoided. In some cases, inactive compounds are synthesized predicted on modeling and then tested to develop a SAR (structure-activity relationship) for compounds interacting with a specific region of MGLL.

One skilled in the art may use one of several methods to screen chemical entities fragments, compounds, or agents for their ability to associate with MGLL and more particularly with the individual binding pockets or active sites of MGLL. This process may begin by visual inspection of, for example, the active site on the computer screen based on the atomic coordinates of MGLL or MGLL complexed with a ligand. Selected chemical entities, compounds, or agents may then be positioned in a variety of orientations, or docked within an individual binding pocket of MGLL. Docking may be accomplished using software such as QUANTA, available from Accelrys, Inc., San Diego, Calif.; and SYBYL, available for Tripos, St. Louis, Mo.; followed by energy minimization and molecular dynamics with standard molecular mechanics forcefields, such as CHARMm; available from Accelrys, Inc., San Diego, Calif.; and AMBER, University of California, San Francisco.

Specialized computer programs may also assist in the process of selecting chemical entities. These include but are not limited to: GRID (Goodford 1985), available from Oxford University, Oxford, UK); MCSS (Miranker and Karplus 1991), available from Molecular Simulations, Burlington, Mass.; AUTODOCK (Goodsell and Olsen 1990), available from Scripps Research Institute, La Jolla, Calif.; and DOCK (Kuntz et al. 1982), available from University of California, San Francisco, Calif.

The use of software such as GRID, a program that determines probable interaction sites between probes with various functional group characteristics and the macromolecular surface, is used to analyze the surface sites to determine structures of similar inhibiting proteins or compounds. The GRID calculations, with suitable inhibiting groups on molecules (e.g., protonated primary amines) as the probe, are used to identify potential hotspots around accessible positions at suitable energy contour levels. The program DOCK may be used to analyze an active site or ligand-binding site and suggest ligands with complementary steric properties.

Once suitable chemical entities, compounds, or agents have been selected, they can be assembled into a single ligand or compound or inhibitor or activator. Assembly may proceed by visual inspection of the relationship of the fragments to each other on the three-dimensional image. This may be followed by manual model building using software such as QUANTA or SYBYL.

Useful programs to aid in connecting the individual chemical entities, compounds, or agents include but are not limited to: CAVEAT (Bartlett et al. 1989); 3D Database systems such as MACCS-3D (Martin 1992), available from MDL Information Systems, San Leandro, Calif.; and HOOK, available from Molecular Simulations, Burlington, Mass.

Several methodologies for searching three-dimensional databases to test pharmacophore hypotheses and select compounds for screening are available. These include the program CAVEAT (Bacon and Moult 1992). For instance, CAVEAT uses databases of cyclic compounds which can act as “spacers” to connect any number of chemical fragments already positioned in the active site. This allows one skilled in the art to quickly generate hundreds of possible ways to connect the fragments already known or suspected to be necessary for tight binding.

Instead of proceeding to build an inhibitor activator, agonist or antagonist of MGLL in a step-wise fashion one chemical entity at a time as described above, such compounds may be designed as a whole or “de novo” using either an empty active site or optionally including some portion(s) of a known molecule(s). These methods include: LUDI (Bohm 1992), available from Biosym Technologies, San Diego, Calif.; LEGEND (Nishibata and Itai 1991), available from Molecular Simulations, Burlington, Mass.; and LeapFrog, available from Tripos Associates, St. Louis, Mo., USA.

For instance, the program LUDI can determine a list of interaction sites into which to place both hydrogen bonding and hydrophobic fragments. LUDI then uses a library of linkers to connect up to four different interaction sites into fragments. Then smaller “bridging” groups such as —CH2— and —COO— are used to connect these fragments. For example, for the enzyme DHFR, the placements of key functional groups in the well-known inhibitor methotrexate were reproduced by LUDI. See also, (Rotstein and Murcko 1993).

Other molecular modeling techniques may also be employed in accordance with this invention. See, e.g., (Cohen et al. 1990). See also, (Navia and Murcko 1992).

Once a compound has been designed or selected by the above methods, the affinity with which that compound may bind or associate with MGLL may be tested and optimized by computational evaluation and/or by testing biological activity after synthesizing the compound Inhibitors or compounds may interact with the MGLL in more than one conformation that is similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the energy of the free compound and the average energy of the conformations observed when the compound binds to MGLL.

A compound designed or selected as binding or associating with MGLL may be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with MGLL. Such non-complementary (e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the inhibitor and MGLL when the inhibitor is bound, preferably make a neutral or favourable contribution to the enthalpy of binding. Weak binding compounds will also be designed by these methods so as to determine SAR.

Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include: Gaussian 92, revision C (Frisch et al. 1992); AMBER, University of California, San Francisco; QUANTA and CHARMm, available from Accelrys, Inc., San Diego, Calif.; and Insight II/Discover, from Biosysm Technologies Inc., San Diego, Calif., USA. Other hardware systems and software packages will be known to those skilled in the art.

Once a compound that associates with MGLL has been optimally selected or designed, as described above, substitutions may then be made in some of its atoms or side groups in order to improve or modify its binding properties. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. It should, of course, be understood that components known in the art to alter conformation may be avoided. Such substituted chemical compounds may then be analyzed for efficiency of fit to MGLL by the same computer methods described in detail, above.

Use of Homology Structure Modeling to Design Ligands with Modulated Binding or Activity to MGLL.

The present invention includes the use of the atomic coordinates and structures of MGLL and/or MGLL complexed with an inhibitor to design modifications to starting compounds and derivatives thereof that will bind more tightly or interact more specifically to the target enzyme.

The structure of a complex between the MGLL and the starting compound can be used to guide the modification of that compound to produce new compounds that have other desirable properties for applicable industrial and other uses (e.g., as pharmaceuticals), such as chemical stability, solubility or membrane permeability. (Lipinski et al. 1997).

Binding compounds, agonists, antagonists and such that are known in the art. Such compounds can be diffused into or soaked with the stabilized crystals of MGLL to form a complex for collecting X-ray diffraction data. Alternatively, the compounds, known and unknown in the art, can be cocrystallized with MGLL by mixing the compound with MGLL before precipitation.

To produce custom high affinity and very specific compounds, the structure of MGLL can be compared to the structure of a selected non-targeted molecule and a hybrid constructed by changing the structure of residues at the binding site for a ligand for the residues at the same positions of the non-target molecule. The process whereby this modeling is achieved is referred to as homology structure modeling. This is done computationally by removing the side chains from the molecule or target of known structure and replacing them with the side chains of the unknown structure put in sterically plausible positions. In this way it can be understood how the shapes of the active site cavities of the targeted and non-targeted molecules differ. This process, therefore, provides information concerning how a bound ligand can be chemically altered in order to produce compounds that will bind tightly and specifically to the desired target but will simultaneously be sterically prevented from binding to the non-targeted molecule. Likewise, knowledge of portions of the bound ligands that are facing to the solvent would allow introduction of other functional groups for additional pharmaceutical purposes. The use of homology structure modeling to design molecules (ligands) that bind more tightly to the target enzyme than to the non-target enzyme has wide spread applicability.

Databases and Computer Systems

An amino acid sequence or nucleotide sequence of MGLL and/or X-ray diffraction data, useful for computer molecular modeling of MGLL or a portion thereof, can be provided in a variety of mediums to facilitate use thereof In one application of this embodiment, databases comprising data pertaining to MGLL, or at least one subdomain thereof, amino acid and nucleic acid sequence and/or X-ray diffraction data of the present invention is recorded on computer readable medium. A skilled artisan can readily appreciate how any of the presently known computer readable media can be used to create a manufacture comprising computer readable medium having recorded thereon an amino acid sequence and/or X-ray diffraction data of the present invention.

A variety of data storage structures are available to a skilled artisan for creating a computer readable medium having recorded thereon an amino acid sequence and/or atomic coordinate/X-ray diffraction data of the present invention. The choice of the data storage structure will generally be based on the means chosen to access the stored information. In addition, a variety of data processor programs and formats can be used to store the sequence and X-ray data information of the present invention on computer readable media. The sequence information can be represented in a word processing text file, formatted in commercially-available software such as WordPerfect and MICROSOFT Word, or represented in the form of an ASCII file, stored in a database application, such as DB2, Sybase, Oracle, or the like. A skilled artisan can readily adapt any number of dataprocessor structuring formats (e.g., text file or database) in order to obtain computer readable media having recorded thereon the information of the present invention.

By providing computer readable media having sequence and/or atomic coordinates based on X-ray diffraction data, a skilled artisan can routinely access the sequence and atomic coordinate or X-ray diffraction data to model a related molecule, a subdomain, mimetic, or a ligand thereof Computer algorithms are publicly and commercially available which allow a skilled artisan to access this data provided in a computer readable medium and analyze it for molecular modeling and/or RDD (rational drug design). See, e.g., (Mary Ann Liebert (Publishers) 1995).

The present invention further provides systems, particularly computer-based systems, which contain the sequence and/or diffraction data described herein. Such systems are designed to do structure determination and RDD for MGLL or at least one subdomain thereof Non-limiting examples are microcomputer workstations available from Silicon Graphics Incorporated and Sun Microsystems running UNIX based, Windows NT or IBM OS/2 operating systems.

A variety of comparing means can also be used to compare a target sequence or target motif with the data storage means to identify structural motifs or electron density maps derived in part from the atomic coordinate/X-ray diffraction data. A skilled artisan can readily recognize that any one of the publicly available computer modeling programs can be used as the search means for the computer-based systems of the present invention.

Integrated Procedures Which Utilize the Present Invention

Molecular modeling is provided by the present invention for rational drug design (RDD) of mimetics and ligands of MGLL. As described above, the drug design paradigm uses computer-modeling programs to determine potential mimetics and ligands which are expected to interact with sites on the protein. The potential mimetics or ligands are then screened for activity and/or binding and/or interaction. For MGLL-related mimetics or ligands, screening methods can be selected from assays for at least one biological activity of MGLL, e.g., such as hydrolysis by MGLL.

Thus, the tools and methodologies provided by the present invention may be used in procedures for identifying and designing ligands which bind in desirable ways with the target. Such procedures utilize an iterative process whereby ligands are synthesized, tested and characterized. New ligands can be designed based on the information gained in the testing and characterization of the initial ligands and then such newly identified ligands can themselves be tested and characterized. This series of processes may be repeated as many times as necessary to obtain ligands with the desirable binding properties.

The following steps (1-7) serve as an example of the overall procedure:

-   1. A biological activity of a target is selected (e.g., hydrolysis     by MGLL). -   2. A ligand is identified that appears to be in some way associated     with the chosen biological activity (e.g., the ligand may be an     inhibitor of a known activity). The activity of the ligand may be     tested by in vivo and/or in vitro methods. A ligand of the present     invention can be, but is not limited to, at least one selected from     a lipid, a nucleic acid, a compound, a protein, an element, an     antibody, a saccharide, an isotope, a carbohydrate, an imaging     agent, a lipoprotein, a glycoprotein, an enzyme, a detectable probe,     and antibody or fragment thereof, or any combination thereof, which     can be detectably labeled as for labeling antibodies. Such labels     include, but are not limited to, enzymatic labels, radioisotope or     radioactive compounds or elements, fluorescent compounds or metals,     chemiluminescent compounds and bioluminescent compounds.     Alternatively, any other known diagnostic or therapeutic agent can     be used in a method of the invention. Suitable compounds are then     tested for activities in relationship to the target. Complexes     between MGLL and ligands are made either by co-crystallization or     more commonly by diffusing the small molecule ligand into the     crystal. X-ray diffraction data from the complex crystal are     measured and a difference electron density map is calculated. This     process provides the precise location of the bound ligand on the     target molecule. The difference Fourier is calculated using measure     diffraction amplitudes and the phases of these reflections     calculated from the coordinates. -   3. Using the methods of the present invention, X-ray crystallography     is utilized to create electron density maps and/or molecular models     of the interaction of the ligand with the target molecule. The entry     of the coordinates of the target into the computer programs     discussed above results in the calculation of most probable     structure of the macromolecule. These structures are combined and     refined by additional calculations using such programs to determine     the probable or actual three-dimensional structure of the target     including potential or actual active or binding sites of ligands.     Such molecular modeling (and related) programs useful for rational     drug design of ligands or mimetics are also provided by the present     invention. -   4. The electron density maps and/or molecular models obtained in     Step 3 are compared to the electron density maps and/or molecular     models of a non-ligand containing target and the observed/calculated     differences are used to specifically locate the binding of the     ligand on the target or subunit. -   5. Modeling tools, such as computational chemistry and computer     modeling, are used to adjust or modify the structure of the ligand     so that it can make additional or different interactions with the     target. The ligand design uses computer-modeling programs which     calculate how different molecules interact with the various sites of     the target, subunit, or a fragment thereof. Thus, this procedure     determines potential ligands or ligand mimetics. -   6. The newly designed ligand from Step 5 can be tested for its     biological activity using appropriate in vivo or in vitro tests,     including the high-throughput screening methods discussed above. The     potential ligands or mimetics are then screened for activity     relating to MGLL, or at least a fragment thereof. Such screening     methods are selected from assays for at least one biological     activity of the native target. The resulting ligands or mimetics,     provided by methods of the present invention, are useful for     treating, screening or preventing diseases in animals, such as     mammals (including humans). -   7. Of course, each of the above steps can be modified as desired by     those of skill in the art so as to refine the procedure for the     particular goal in mind Also, additional X-ray diffraction data may     be collected on MGLL, MGLL/ligand complexes, MGLL structural target     motifs and MGLL subunit/ligand complexes at any step or phase of the     procedure. Such additional diffraction data can be used to     reconstruct electron density maps and molecular models, which may     further assist in the design and selection of ligands with the     desirable binding attributes.

It is to be understood that the present invention is considered to include stereoisomers as well as optical isomers, e.g., mixtures of enantiomers as well as individual enantiomers and diastereomers, which arise as a consequence of structural asymmetry in selected compounds, ligands or mimetics of the present series.

Some of the compounds or agents disclosed or discovered by the methods herein may contain one or more asymmetric centers and thus give rise to enantiomers, diastereomers, and other stereoisomeric forms. The present invention is also meant to encompass all such possible forms as well as their racemic and resolved forms and mixtures thereof When the compounds described or discovered herein contain olefinic double bonds or other centers of geometric asymmetry, and unless otherwise specified, it is intended to include both E and Z geometric isomers. All tautomers are intended to be encompassed by the present invention as well.

Examples

Without further description, it is believed that one of ordinary skill in the art can, using the preceding description and the following illustrative examples, make and utilize the present invention and practice the claimed methods. The following working examples therefore, specifically point out preferred embodiments of the present invention, and are not to be construed as limiting in any way the remainder of the disclosure.

BLAST Search and Sequence Alignment

The reference sequences for MGLL Isoform 2 (Karlsson et al. 2001) and Isoform 1 (Wall et al. 1997) are shown in FIG. 1: A and FIG. 1: B, respectively. Note that the sequences of MGLL Isoform 2 and MGLL Isoform 1 are 100% identical, except that MGLL Isoform 1 has an additional 10 amino acids at the N-terminus The alignment for MGLL Isoform 2 and MGLL Isoform 1 is shown in FIG. 1: C. The numbering of amino acids for MGLL Isoform 2 (SEQ ID NO: 1) was used throughout the following description to refer to amino acids in the engineered constructs of the present invention.

A BLAST search (Altschul et al. 1990) against the sequence data set deposited in the Protein Data Bank (Sussman et al. 1998) was conducted to identify a protein of known crystal structure with reasonable sequence homology to MGLL. The closest relative to MGLL found in the Protein Data Bank was RsbQ, a stress-response regulator in Bacillus subtilis (Kaneko et al. 2005). RsbQ shares 25% sequence identity with human MGLL. RsbQ also had the highest sequence identity and smallest insertions and deletions relative to MGLL of any structure available in the PDB at the time of this work. The protein RsbQ, PDB ID 1wom (Kaneko et al. 2005), was used as a template. The sequences of RsbQ and MGLL isoform 2 were aligned using the ClustalW software (Thompson et al. 1994; Higgins et al. 1996). RsbQ is a α/β hydrolase with a catalytic triad composed of Ser96, His247 and Asp219. The Asp-His-Ser catalytic triad of MGLL matched the corresponding residues in RsbQ. This alignment was duplicated within the GeneMine software (Lee and Irizarry 2001) and adjusted to eliminate insertions or deletions within elements of secondary structure without disturbing the alignment of the catalytic residues. The final alignment of human MGLL isoform 2 and RsbQ is shown in FIG. 2A. Although the sequence identity between MGLL and RsbQ is low for generating a homology model for MGLL, it was estimated that a low accuracy model would be sufficient to identify hydrophobic residues in the outside of the molecule that could trigger aggregation.

Homology Model

A homology model of MGLL was created using RsbQ as a template and the “quick refine” option in GeneMine software (FIG. 2A) (Levitt 1992) (Lee and Irizarry 2001). The model shows a α/β hydrolase domain and a cap-domain composed of 4 helices. Helix 151-185 of the cap-domain shows amphiphilic properties, characteristic of proteins involved in lipid binding. The helix contains a slight bend due to the presence of a proline residue at position 172. 14 out of the 32 residues constituting the helix are hydrophobic (FIG. 2A). 7 of the hydrophobic residues are Leucines (Leu 152, 157, 159, 171, 174, 176, 184). In the model, the side chains of Leu 159 and 176 point towards the solvent, possibly constituting a recognition site for the interaction of MGLL with the membrane. It should be noted that because of the low accuracy of the model, other Leucine residues, whose side chains appear to point toward the core of the molecule in the homology model, may also contribute to the hydrophobic properties of MGLL and trigger the need for detergent.

Construct Design

A library of constructs was designed in an effort to generate MGLL protein that would be less prone to aggregation, not require detergent for purification, and be more suitable for high-throughput screening and crystallization. A total of 52 mut-MGLL constructs were generated by mixing and matching the cap-domain mutations, surface mutations, and truncations (Table 1). Seven different hydrophobic Leucine residues (designated as Leu or L) of the cap-domain were selected for mutations (Leu 162, 167, 169, 171, 174, 176, and 184). The Leucine residues were replaced by Serine (designated as Ser or S), Glutamine (designated as Gln, or Q), or Arginine (designated as Arg or R). In addition, eight Lysine residues (designated as Lys or K) were identified at the surface of the MGLL homology model (Lys 36, 160, 165, 188, 206, 226, 259 and 269) and were mutated to Alanine (designated as Ala or A) to increase crystal contacts, promote crystallization, and improve crystal quality. The surface mutations were introduced into the mut-MGLL (hMGLL 1-303 L169S, 176S) double cap-domain mutant construct either independently or in combination with other surface mutations. N-terminal and C-terminal truncation constructs were also designed (Table 1). The N-terminus was truncated at amino acid 9, 19, 26, and 33. The C-terminus was truncated at 297 and 292. The N-terminal and C-terminal truncations were introduced independently or combined with other truncations and were introduced into the mut-MGLL (hMGLL 1-303 L169S, 176S) double cap-domain mutant construct (Table 1). All constructs, including the wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) construct, were engineered with an N-terminal histidine tag (His tag) followed by a TEV protease cleavage site so that the tag could be cleaved after purification. TEV is highly site-specific protease that is found in the Tobacco Etch Virus (Invitrogen).

Cloning

The cDNA for MGLL was cloned from human brain DNA and used as a template to generate a PCR fragment of full-length wt-MGLL corresponding to amino acids 1-303 of the reference sequence for human MGLL Isoform 2 (SEQ ID NO: 1) The sequences for the 3′ and 5′ PCR primers are shown below.

5′ primer: gagaatttggtattttcaaggtatgccagaggaaagttcccc 3′ primer: tggatgtgtatgtttctatcagggtggggacgaagttcc

The PCR product was purified (GENECLEAN SPIN kits, Qbiogene, Inc), treated with T4 polymerase (New England Biolabs), ligated into the modified pENTR.11cLIC vector, and transformed into TOP10 one shot competent cells (Invitrogen). After sequence confirmation, the mutations were added by Quickchange mutagenesis, (Stratagene). The sequence confirmed plasmids were purified for transfection into insect cells using the BaculoDirect Baculovirus Expression System (Invitrogen). All of the resulting proteins contained an N-terminal His tag followed by a TEV cleavage site and the amino acids of the different MGLL constructs. Viral stock was propagated for two more amplifications at a low multiplicity of infection (MOI) to render a P2 virus stock.

Recombinant Production of wt-MGLL and mut-MGLL

Large-scale expression was carried out in 2-liter shake flasks or WAVE bioreactors (WAVE Products Group, GE Healthcare). The P2 virus was expanded to generate a high titer P3 stock by infecting Sf9 cells in suspension at MOI of 0.3 and harvesting the virus after 72 hours. Cell paste for wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) and mut-MGLL were obtained by infecting Sf9 cells at a density of 1.5×10⁶ cells/ml with a MOI of 1. Infected cultures were maintained at 27° C. under constant shaking at 140 rpm. Cells were harvested 65-72 hours post-infection by centrifugation at 1000×g for 10 minutes at 4° C. Cell viability were determined by Guava ViaCount or Trypan Blue and routinely were between 60 and 80% at time of harvest. Cell pellets were washed once in phosphate-buffered saline with broad range protease inhibitors and stored at −80° C.

Purification of Wild-Type MGLL (wt-MGLL)

A pilot purification of wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3), performed in the complete absence of detergent, generated no protein (data not shown). A second purification of wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) was done with detergent in the lysis buffer only. Frozen cell pellets for wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) were thawed, resuspended, and lysed in Bugbuster® lysis buffer for 1 hour at 4° C. Bugbuster® lysis buffer is a proprietary lysis buffer from Invitrogen that contains detergent. The lysate was clarified by centrifugation at 40,000×g for 1 hr. No detergent was added at this point or during the rest of the purification. From this point forward, the purification protocol and buffers were the same as described below for mut-MGLL. An average of 2.2 mg of wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) per liter of cell culture was obtained. Further analysis by size exclusion chromatography showed complete aggregation of the purified wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3), which confirmed the need for detergent for wt-MGLL purification as previously described in the literature.

Purification of mut-MGLL

Mutant MGLL (mut-MGLL) constructs were purified in the absence of detergent. Frozen cell pellets were thawed and resuspended in Buffer A (50 mM Hepes buffer pH 7.5, 400 mM NaCl, 5% glycerol, 0.05% BME, 1× Complete EDTA-free protease inhibitor cocktail tablets (Roche)), dounce homogenized and mechanically lysed with a microfluidizer processor (Microfluidics). The extract was clarified by centrifugation at 40,000×g for 1 hr. The cleared lysate was loaded on a 1 ml His-Trap FF Crude column (GE-Healthcare) at 4° C. using the AktaXpress system. For larger preparations, a 5 ml His-Trap FF Crude column was used. The column was washed with 10-15 column volumes (CV) of buffer A containing 30 mM imidazole and mut-MGLL was eluted with 5 CV of 50 mM Hepes buffer pH 7.5, 400 mM NaCl, 5% glycerol, 0.05% BME, 400 mM imidazole. In most preparations, 30 mM imidazole was included in Buffer A from the beginning of the preparation to reduce non-specific binding on the His-Trap column. In addition, a slightly lower imidazole concentration of 350 mM was used in the final elution during later preparations to further improve purity. Glycerol concentration was also reduced to 4% to avoid back pressure problems on the AktaXpress, after it was determined that mut-MGLL constructs were stable in 2% glycerol. The elution peak was directly loaded on a Superdex 200 HR 16/60 preequilibrated with 50 mM Hepes pH7.5 buffer containing 200 mM NaCl, 2% glycerol, 2 mM DTT, 2 mM EDTA. Fractions were analysed by SDS-PAGE. Fractions containing mut-MGLL were pooled. Purification yields were determined by Bradford assay using the protein assay kit from BioRad according to manufacturer's instruction with BSA as a standard (Bradford 1976).

The majority of constructs containing N-terminal and/or C-terminal truncations did not have high enough expression to allow for purification of soluble protein (Table 1).

Constructs that were evaluated containing just the cap-domain mutations generated between 0.7 and 4.5 mg/L, except the mut-MGLL construct containing the L174Q mutation, which showed no expression (Table 1). Analysis by size exclusion chromatography showed that the purified mut-MGLL proteins were 90% monomeric and only 10% aggregated compared to 100% aggregation for wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) (FIG. 1A), which indicated that the mutations significantly improved protein solubility and eliminated the need for detergent during purification.

Constructs that were evaluated with a combination of cap-domain and surface mutations showed expression levels between 0.5 and 3.6 mg/L and were also ˜90% monomeric on SDS Page as well (data not shown).

TEV Cleavage

To remove the N-terminal His tag, 0.2 units of TEV Protease for each ug of mut-MGLL were added to the mut-MGLL pool. The reaction was done overnight at 4° C. Cleavage of the histidine tag was monitored by SDS-PAGE.

Complex Formation

For crystallization trials, compounds were added in a 1:2 molar ratio (mut-MGLL: compound). TEV protease cleaved mut-MGLL was first diluted to 0.3 mg/ml with buffer containing 50 mM Hepes pH 7.5, 200 mM NaCl, 2% Glycerol, 2 mM DTT, and 2 mM EDTA. Compounds were added to the diluted protein and the mixture was incubated overnight at 4° C. After the overnight incubation, the mixture was concentrated to a final protein concentration of 6.0 mg/ml using a Ultrafree membrane (10 KDa cut-off). At this stage the purity was >98% as determined by SDS-PAGE and the protein was ready for crystallization trials.

Circular Dichroism (CD)

One construct, TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S) (SEQ ID NO: 5), was selected for further characterization by CD to ensure that the mutations introduced did not adversely affect protein conformation and activity. Circular dichroism experiments were performed on a Circular Dichroism Spectrometer Model 202 from Aviv Instruments Inc. The CD scans of wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) and TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S) (SEQ ID NO: 5) (5 μM protein in 10 mM cacodylic acid pH 7 and 140 mM NaCl) were measured from 200 to 260 nm. Temperature melts were monitored at 210 nm. The CD spectra were converted to molar ellipticity and are shown in FIG. 1B.

The CD scans for the wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) purified in the presence of detergent and TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S) (SEQ ID NO: 5) were similar indicating that the two enzymes had a similar conformation (FIG. 1B). The scans were characteristic of proteins with high alpha-helical content as expected for a lipase.

Kinetic Analysis

To ensure that the mutations engineered did not adversely affect protein activity, a number of the newly generated MGLL mutants were analyzed using by enzyme assay and then compared to wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3). A small fluorescent substrate, 4-methyl coumarin butyrate (4MC-B) was used to compare the activity of the engineered mutants to the activity of wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3). The catalytic efficiency (k_(cat)/K_(M)) for the hydrolysis of the 4MC-B was similar for wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) and all MGLL mutants tested (Table 2). A larger more aliphatic fluorescent substrate, Coumarin Arachidonate (C-A), structurally more closely related to the MGLL natural substrate, 2-AG, was used to compare the activity of wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) to TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S) (SEQ ID NO: 5). The catalytic efficiency for the hydrolysis of the C-A substrate was equivalent between wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) and TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S) (SEQ ID NO: 5), which confirmed that the mutations did not affect MGLL activity (Table 2).

The Michaelis-Menten parameters for the hydrolysis of 4-methylcoumarin butyrate (4MC-B) and coumarin arachidonate (C-A) substrate were determined using 4-5 nM of MGLL in 20 mM Pipes pH 7 and 150 mM NaCl at 37° C. The change in fluorescence due to substrate hydrolysis was monitored using excitation/emission wavelengths of 335/440 in a Safire II instrument from Tecan. The hyperbolic rates versus substrate concentration curves for the hydrolysis of 4MC-B were fit to the Michaelis-Menten equation using Excel.

$v = \frac{V_{\max}*\lbrack S\rbrack}{K_{M} + \left\lbrack S \right\}}$

The solubility limit of coumarin arachidonate (C-A) substrate did not allow for the determination of K_(M) and k_(cat). The apparent k_(cat)/K_(m) ratio for the hydrolysis of C-A was determined at [S]<<K_(M). The apparent K_(M) for C-A was estimated to be >30 μM. The k_(cat)/K_(M) values reported are the average from independent values determined from five substrate concentrations ranging from 700 to 40 nM.

Thermal Stability

The Thermofluor® assay is a powerful tool to screen for small molecule inhibitors interacting with a protein's active site or allosteric site. The assay detects small changes in the intrinsic melting temperature of proteins based on binding of ligands. Compounds that interact preferentially with the native form of the protein will increase the T_(m), the temperature at which half of the protein is unfolded (Pantoliano et al. 2001). The technique monitors changes in the fluorescent intensity of dyes such as 1-anilinonaphthalene-8-sulfonic acid (1,8-ANS). The fluorescent dyes are quenched in aqueous environments but increase in fluorescence on binding to the hydrophobic core of denatured proteins.

Thermofluor® assays were conducted to characterize wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) and mut-MGLL (hMGLL 1-303 L169S, L176S) and evaluate if the MGLL mutants could be used for high-throughput screening using Thermofluor®. Three microliters of protein at a concentration of 0.05 mg/ml in 50 mM Pipes pH 7, 200 mM NaCl, 100 μM 1,8-ANS, and 0.001% Tween was added to pre-dispensed compound plates. Wells were overlaid with silicone oil (1 μL, Fluka, type DC 200) to prevent evaporation. Final compound concentrations varied from 150 to 0.15 μM. Assay plates were heated at a rate of 1° C./min for all experiments over a temperature range sufficient to measure protein unfolding. Fluorescence was measured by continuous illumination with UV light (Hamamatsu LC6) supplied via fiber optic and filtered through a custom band-pass filter (380-400 nm; >6 OD cutoff). Fluorescence emission was detected by measuring light intensity using a CCD camera (Sensys, Roper Scientific) filtered to detect emission at 500±25 nm, resulting in simultaneous and independent readings of all 384 wells. One or more images were collected at each temperature, and the sum of the pixel intensity in a given area of the assay plate was recorded vs temperature, and fit to standard equations to yield the T_(m).

The study using Thermofluor® showed that wt-MGLL (hMGLL 1-303) (SEQ ID NO: 3) had a very poor transition, characteristic for aggregated or unfolded proteins (FIG. 5). TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S) (SEQ ID NO: 5), however, gave a strong transition with a T_(m) value of 56.7° C., indicating that the engineered mutation produced a more soluble MGLL protein that was suitable for high-throughput screening.

Crystallization

All mutants were purified according to the procedure described above and submitted for crystallization trials. Purity greater than 95% as determine by SDS Page was achieved for all constructs. Combinations of high-throughput and manual crystallization screens were used. Apo proteins generated crystals diffracting between 8.0 Å and 9.0 Å only, despite extensive optimization trials. Co-crystallization with methyl arachidonyl fluorophosphonate (MAFP) did not significantly improve diffraction.

Co-crystallization of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) with Compound 1 generated crystals that diffracted to 2.3 Å, but with diffused scattering in one orientation. Further optimization experiments did not improve data quality with that complex. High quality diffraction was achieved by co-crystallization of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) with Compound 2, a compound that was 10 fold more potent than Compound 1. Crystallization of the TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) and Compound 2 complex was achieved at 22° C. with a hanging droplet containing an approximately 6 mg/ml protein solution combined with a modified well solution containing 8% polyethylene glycol monomethyl ether 5000 molecular weight (PEG MME 5K), 100 mM Na Citrate pH 5.5 and 2% n-Octyl-Beta-D-Glucopyranoside (OBG), which was suspended over a well solution containing 6% PEG MME 5K, 100 mM Na Citrate pH 5.5 and 2% OBG. Crystals, however, were not generated spontaneously. A seed solution generated from poor quality crystals obtained previously was used to seed crystallization droplets. The optimal volume ratios in the drop for obtaining good quality crystals were 1 ul protein solution, 0.5 ul modified well solution, and 0.2 ul diluted seed stock solution. Any increase in protein concentration resulted in heavy showers and stacked plate crystals despite adjustments in crystallization reagent concentration. Protein supplied at concentrations higher than 6 mg/ml and diluted to 6 mg/ml before crystallization trials also resulted in heavy crystal showers. Final resolution was 1.3 Å for the TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) and Compound 2 complex.

A crystal lead was also identified with a high-throughput method using TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) in complex with Compound 3. Crystal conditions were reproduced at 22° C. with a hanging droplet containing an approximately 6 mg/ml protein solution combined with an equal volume, usually 1 ul, of well solution containing 15% PEG 4000 and 120 mM LiCl, which was suspended over a reservoir containing 1 ml of the same well solution.

Structure Determination

Crystals of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) in complex with Compound 2 were harvested, transferred to 16% PEG MME 5K, 100 mM Na-MES pH 6.0, 25% glycerol and flash frozen in liquid nitrogen. Datasets were collected on a Rigaku M007HF generator at 100K or at the ID19 beamline at IMCA-CAD at the Advanced Photon Source, Chicago. A summary of the data-collection statistics is in Table 3. The data was processed in the HKL2000 suite (Otwinowski and Minor 1997) and the structure was solved by molecular replacement using a modified structure of “Non-haem bromoperoxidase BPO-A1” (PDB ID 1A8Q) as search model in PHASER (McCoy et al. 2007). The initial rebuilding was performed using the default protocol in the AutoBuild Wizard in PHENIX (Adams et al. 2002; Adams et al. 2004; Terwilliger et al. 2008), refinement and automated water picking was carried out in PHENIX.refine (Adams et al. 2002; Adams et al. 2004; Terwilliger et al. 2008); Coot (Emsley and Cowtan 2004) was employed for model building, ligand placement and manual assignment of water molecules. Ligand restraints were generated in PHENIX.elbow (Adams et al. 2002; Adams et al. 2004) and the final model validated using tools implemented in Coot; Figures were generated in PyMol (DeLano 2002). Coordinates for the structure of the complex of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) with Compound 2 are included as Table 6.

For TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) in complex with Compound 3, a single usable crystal was harvested, transferred to 19% PEG 4000, 120 mM LiCl, 30% glycerol and flash frozen in liquid nitrogen. A complete dataset was collected on a Rigaku M007HF generator at 100K. A summary of the data-collection statistics is in Table 4. The structure was solved by molecular replacement in PHASER using the previously determined structure of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) in complex with Compound 2 as a search model. The C2 crystal form obtained with Compound 3 exhibits two molecules in the asymmetric unit as compared to one molecule in the C222₁ form obtained with Compound 2. Model building and refinement proceeded as described earlier in this text. The model exhibits only mediocre geometry owing to poor diffraction quality of the crystal and increased flexibility in parts of the molecule. Coordinates for the structure of the complex of TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) with Compound 3 are included as Table 7.

Overall Structure of MGLL

MGLL is part of the sub-family of lipid hydrolases, which in turn is part of a larger family of α/β-hydrolases with diverse catalytic functions. Members of this super-family include: ester hydrolases, lipid hydrolases, thioester hydrolases, peptide hydrolases, haloperoxidases, dehalogenases epoxide hydrolases and C—C bond breaking enzymes (Holmquist 2000). All of these enzymes share a common folding motif called the α/β-hydrolase fold (Ollis et al. 1992; Heikinheimo et al. 1999). This fold is characterized by eight β-sheets flanked on both sides by α-helices. β-sheet 2 is antiparallel to the other sheets and the first and last helix (α1 or αA and α6 or αF) are located on one side of the sheets, whereas the remainder of the helices are present on the opposite side. The α/β-hydrolase fold tolerates a vide variety of inserts without losing the core folding motif These inserts serve to modify and regulate the catalytic activity of the respective proteins. They can occur in several locations, but are mostly located in a loop region between strand β6 and helix α6.

Herein is described the structure of the inhibitor bound form of human MGLL Isoform 2 (TEV protease cleaved mut-MGLL (hMGLL 1-303 L169S, L176S, K36A) (SEQ ID NO: 7) with Compound 2), which has been determined by molecular replacement to a resolution of 1.3 Å. The structure of MGLL conforms very closely to the canonical α/β-hydrolase fold. The structure is characterized by eight β-sheets, which form a partial β-barrel adorned on both sides with eight α-helices. MGLL contains two additional helices (α4 (αD′₁) and α5 D′₂)), which are part of the cap-domain and are inserted in the protein sequence between sheet β6 and helix α6 (αD). Helices α1 (αA) and α8 (αF) are located on the concave side of the barrel and helices α2 (αB), α3 (αC), α6(D) and α7(E) are on the convex side. Both cap-domain helices are oriented in front of the molecule perpendicular to the plane of the β-barrel.

Interestingly the overall structure of this mammalian MGLL is closer to bacterial lipases than any mammalian lipase when the structure is compared to the latest release of the Protein Databank using the protein structure-matching tool (SSM) at the European Institute of Bioinformatics (EBI) (Boutselakis et al. 2003). The 3D-alignment produces several close hits against bacterial Bromoperoxidases, Chloroperoxidases and Arylesterases. The same hits were also produced by a PHI-blast search of the Protein Databank against the protein sequence alone. Since no similar 3D-hits were found against any diacylglycerol lipases or triacylglycerol lipases, it can be inferred that the structural requirements for cleavage of triacylglycerol and diacylglycerol esters are substantially different from those required for the cleavage of mono-glycerol esters. It appears as if these classes of proteins, even though they perform similar functions, represent a different branch on the evolutionary tree of lipases.

Superposition of several hits from the 3D-alignment (Chloroperoxidase L, PDBID:1A88; Bromoperoxidase A1, PDBID:1A8Q; P. putida Esterase, PDBID:1ZOI; Gamma Lactamase, PDBID:1HKH) shows that the α/β-hydroxylase core without the cap-domain superimposes very well (Table 5 and FIG. 10). The largest differences are seen in the first 20 residues of the N-terminus of MGLL, for which there is no complement in the other proteins. Further differences are evident in helix α6 (D). In MGLL α6 continuously spans approximately 20 residues, whereas in the other structures it is partially unraveled and split into two pieces connected by a short loop.

MGLL Binding Pocket

Compound 2 is bound in an extended and closed binding pocket, which is located between helices α4, α6, α7 and α5. Even though the solvent accessible surface area of the compound (712 Å²) is fairly large, it is almost completely enclosed by the protein. The protein accomplishes this by employing a so-called “cap-domain”, “lid”, or “flap”, which regulates access to the binding site based on the membrane bound state of the protein. The cap-domain is compromised of residues from helices α4 to α5 (also referred to as αD′₁ and αD′₂ throughout the literature). The catalytic triad of MGLL consists of residues Ser122, Asp239, His269 and is located in the center of the binding pocket. The catalytic nucleophile Ser122 resides on a tight turn between strand β5 and helix α3, which is also commonly referred to as the “nucleophilic elbow”. The structurally conserved network of hydrogen-bond donors, which comprises the nucleophilic elbow and the loop connecting α1 and β3 (Gly50, Ala51, Met123 and Gly124) is called the oxyanion hole and serves to stabilize the anionic transition state of the catalytic reaction. The amide carbonyl of Compound 2 points into the oxyanion hole and forms a critical hydrogen bond with the backbone amide nitrogen of Met123 adjacent to the catalytic Serine. The azetidine-piperazine-pyrazine part of the ligand projects into a narrow amphiphilic pocket and fills the available space almost completely. This portion of the ligand does not participate in hydrogen bond interactions with the protein, but one of the pyrazine nitrogens forms an H-bond to a water-network involving two buried water molecules and the side-chains of residues Glu53, Arg57 and His272. A face-to-face π-stacking interaction with of the pyrazine ring with Tyr194 provides further interaction energy.

The binding pocket on the benzoxazole-cyclohexane site of the ligand is less occluded than its counter part on the opposite site. The benzoxazole portion of the ligand is located in a hydrophobic environment constituted mainly from side chains of aliphatic residues. The cyclohexane portion projects into a more spacious void, and along with the benzoxazole, is the only part of the inhibitor, which is accessible by solvent in the protein bound state. These parts of the ligand form mostly van der Waals interactions with the protein. The cyclohexane part of the molecule is less well ordered than the remainder of the ligand. This can be explained by the fact that this region of the cap-domain (α4 and part of the loop connecting to α5) with which the inhibitor interacts, is displays significantly higher temperature factors as compared to the rest of the protein. The elevated temperature factors signify the inherent flexibility of this region, which probably facilitates its displacement from the surface of the protein during ligand binding and release.

Compound 3 is bound in the same pocket as Compound 2. As observed in the case of Compound 2, the canonical interaction of an amide carbonyl with the backbone of Met123 in the oxyanion hole is conserved. The compound assumes an almost triangular shape in the binding pocket with the tetrazole ring pointing towards Arg57 and forming a hydrogen bond with its sidechain. The methyl-benzylamide points into the hydrophobic pocket and participates mostly in van der Waals interactions. The methylthiopene ring is halfway tucked under the benzylamide portions, with both ring systems being almost parallel to each other. The difference in the shape of the compound causes extensive rearrangement in the lid region and the connecting loop regions. Helix α4 and the connecting loop to α5 show substantial disorder and account for much of the bad geometry observed in the structure. In general, the protein in this C2 crystal form is less well ordered and exhibits higher thermal factors as compared to the C222₁ form.

Enabling Mutations

In order to obtain the MGLL structure several enabling mutations were required. Two mutations in the lid sub-domain (L169S and L176S) helped to increase solubility of the protein enough to prevent aggregation and to eliminate the need for detergents in protein purification. L169S is located at the C-terminal end of helix α4 (αD′₁) and L176S on a loop connecting α4 to α5. Interestingly, the cap-domain in the engineered protein still contains quite a few surface exposed aliphatic residues, but the mutations are apparently sufficient to reverse the inherent lipophilic character of the protein enough to prevent aggregation in solution.

The K36A surface mutation was inspired by a series of reports indicating that the replacement of flexible residues with high conformational entropy present on the surface of proteins helps to promote crystallization under certain circumstances (Longenecker et al. 2001; Mateja et al. 2002). The K36A mutation is present on a loop connecting sheets β2 and β3. This loop interacts with the cap-domain of a neighboring symmetry related molecule between Val170 and Pro172. Analysis of this packing interaction reveals that the Lysine would have fit snuggly into this packing interface, so the immediate reason necessitating its absence for crystallization is not obvious.

The mutation appears nevertheless to be beneficial, since this particular part of the cap-domain exhibits relatively high temperature factors and is less well ordered than other parts of the molecule. It is conceivable that this high dynamic mobility would cause the lid to clash into Lys36 in certain parts of the conformational pool. The K36A mutation would eliminate this potential for clashes and may thus contribute to the successful crystallization of the molecule.

Tables

TABLE 1 Engineered forms of MGLL Purification yield mg/L Cap Mutations mut-MGLL (1-303) L169S, L176S 4.5 mut-MGLL (1-303) L167Q 2.3 mut-MGLL (1-303) L171Q 0.7 mut-MGLL (1-303) L174Q 0 mut-MGLL (1-303) L167Q, L171Q 5 mut-MGLL (1-303) L167Q, L174Q 7 mut-MGLL (1-303) L171Q, L174Q 1.5 mut-MGLL (1-303) L167Q, L171Q, L174Q 0 mut-MGLL (1-303) L169Q, L176Q *N.D. mut-MGLL (1-303) L169S *N.D. mut-MGLL (1-303) L176S *N.D. mut-MGLL (1-303) L162S *N.D. mut-MGLL (1-303) L162Q *N.D. mut-MGLL (1-303) L162R *N.D. mut-MGLL (1-303) L184S *N.D. mut-MGLL (1-303) L184Q *N.D. mut-MGLL (1-303) L184R *N.D. mut-MGLL (1-303) L169S *N.D. mut-MGLL (1-303) L169Q *N.D. mut-MGLL (1-303) L169R *N.D. mut-MGLL (1-303) L176S *N.D. mut-MGLL (1-303) L176Q *N.D. mut-MGLL (1-303) L176R *N.D. mut-MGLL (1-303) L167S *N.D. mut-MGLL (1-303) L167R *N.D. mut-MGLL (1-303) L171S *N.D. mut-MGLL (1-303) L171R *N.D. mut-MGLL (1-303) L174S *N.D. mut-MGLL (1-303) L174R *N.D. Cap Mutations + Surface Mutations mut-MGLL (1-303) L169S, L176S, K36A 3.6 mut-MGLL (1-303) L169S, L176S, K160A 0.7 mut-MGLL (1-303) L169S, L176S, K165A 0.5 mut-MGLL (1-303) L169S, L176S, K226A 2.3 mut-MGLL (1-303) L169S, L176S, K36A, K226A 1.5 mut-MGLL (1-303) L169S, L176S, K36A, K188A *N.D. mut-MGLL (1-303) L169S, L176S, K36A, K206A *N.D. mut-MGLL (1-303) L169S, L176S, K36A, K269A *N.D. mut-MGLL (1-303) L169S, L176S, K188A *N.D. mut-MGLL (1-303) L169S, L176S, K206A *N.D. mut-MGLL (1-303) L169S, L176S, K259A *N.D. Cap Mutations + Truncations mut-MGLL (9-303) L169S, L176S 2 mut-MGLL (9-297) L169S, L176S 1 mut-MGLL (1-292) L169S, L176S 0.5 mut-MGLL (19-303) L169S, L176S 0 mut-MGLL (19-297) L169S, L176S 0 mut-MGLL (19-292) L169S, L176S 0 mut-MGLL (26-303) L169S, L176S 0 mut-MGLL (26-297) L169S, L176S 0 mut-MGLL (26-292) L169S, L176S 0 mut-MGLL (33-303) L169S, L176S 0 mut-MGLL (33-297) L169S, L176S 0 mut-MGLL (33-292) L169S, L176S 0 *N.D. is Not Determined

TABLE 2

K_(M) K_(cat) K_(cat)/K_(M) Construct (uM) (uM⁻¹min⁻¹) (uM⁻¹min⁻¹) wt-MGLL.1-303 162 68 0.42 Cap mutants mut-MGLL. 1-303, L169S, L176S 136 48 0.35 mut-MGLL 9-303, L169S, L176S 88 27 0.31 mut-MGLL 9-297, L169S, L176S 126 26 0.21 mut-MGLL 1-303, L171Q 105 51 0.48 mut-MGLL 1-303, L167Q, L171Q 84 59 0.71 mut-MGLL. 1-303, L167Q, L174Q 84 70 0.83 mut-MGLL 1-303, L171Q, L174Q 89 47 0.52 Cap + Surface mutants mut-MGLL 1-303, L169S, L176S, K36A 124 51 0.41 mut-MGLL.1-303, L169S, L176S, K160A 90 30 0.33 mut-MGLL.1-303, L169S, L176S, K165A 137 27 0.2  mut-MGLL 1-303, L169S, L176S, K226A 110 38 0.35 mut-MGLL 1-303, L169S, L176S, K36A, 123 30 0.25 K226A

K_(cat)/K_(M) Construct (uM⁻¹min⁻¹) wt-MGLL 1-303 0.09 mut-MGLL 1-303, L169S, L176S 0.1 

TABLE 3 mut-MGLL complex with Compound 2 Data collection Wavelength (Å) 1.0 Resolution (Å) 1.3 Space group C222₁ Unit cell parameters (Å) a = 93.95, b = 128.45, c = 60.6 No. of reflections 336035 No. of unique reflections 79954 Redundancy 4.2 (1.8) Completeness (%) 89.2 (53.3) R_(merge)  6.2 (31.9) I/σ(I) 19.0 (1.75) Refinement No. of reflections 75577 No. of reflections in R_(free) set 1896 Total No. of non H atoms 2720 No. of protein atoms 2320 No. of ligand atoms 33 No. of solvent molecules 377 R-factor (%) 17.8 R_(free) (%) 20.6 R.M.S. Deviation from ideal geometry Bonds (Å) 0.006 Angles (°) 1.050 B-factors (Å²) Protein 14.8 Ligand 10.2 Ramachandran Plot Preferred Regions (%) 96.6 Allowed regions (%) 3.0 Disallowed regions (%) 0.4

TABLE 4 mut-MGLL complex with Compound 3 Data collection Wavelength (Å) 1.54178 Resolution (Å) 3.0 Space group C2 Unit cell parameters (Å) a = 128.6, b = 72.0, c = 65.2 No. of reflections 34491 No. of unique reflections 11843 Redundancy 2.9 (2.1) Completeness (%) 95.6 (91.9) R_(merge) 13.6 (63.6) I/σ(I)  7.8 (1.11) Refinement No. of reflections 9937 No. of reflections in R_(free) set 479 Total No. of non H atoms 4419 No. of protein atoms 4293 No. of ligand atoms 56 No. of solvent molecules 70 R-factor (%) 25.2 R_(free) (%) 33.8 R.M.S. Deviation from ideal geometry Bonds (Å) 0.007 Angles (°) 1.085 B-factors (Å²) Protein (Chain A) 19.5 Protein (Chain B) 27.8 Ligand 6.1 Ramachandran Plot Preferred Regions (%) 80.8 Allowed regions (%) 14.4 Disallowed regions (%) 4.7

TABLE 5 Chloroper- Bromoper- P. fluorescens Gamma oxidase L oxidase A1 Arylesterase Lactamase Distance [Å] 1.23 1.27 1.29 1.44 No. of matching 168 165 175 173 residues

TABLE 6 CRYST1 93.947  128.145  60.602  90.00  90.00  90.00 C 2 2 21 SCALE1 0.010644 −0.000000 −0.000000 0.00000 SCALE2 0.000000 0.007804 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016501 0.00000 ATOM 1 N PRO A 7 −24.135 50.110 −0.751 1.00 38.62 N ATOM 2 CA PRO A 7 −24.819 48.812 −0.835 1.00 48.66 C ATOM 3 C PRO A 7 −23.834 47.683 −1.121 1.00 27.13 C ATOM 4 CB PRO A 7 −25.762 48.987 −2.031 1.00 56.71 C ATOM 5 CG PRO A 7 −25.901 50.460 −2.210 1.00 69.43 C ATOM 6 CD PRO A 7 −24.588 51.041 −1.797 1.00 66.62 C ATOM 7 O PRO A 7 −23.163 47.709 −2.152 1.00 27.37 O ATOM 8 N ARG A 8 −23.737 46.710 −0.219 1.00 19.22 N ATOM 9 CA ARG A 8 −22.858 45.567 −0.448 1.00 17.80 C ATOM 10 C ARG A 8 −23.445 44.739 −1.589 1.00 10.71 C ATOM 11 CB ARG A 8 −22.696 44.715 0.818 1.00 16.23 C ATOM 12 CG ARG A 8 −22.085 45.452 2.003 1.00 25.04 C ATOM 13 CD ARG A 8 −20.586 45.608 1.857 1.00 23.77 C ATOM 14 NE ARG A 8 −19.862 44.389 2.217 1.00 19.99 N ATOM 15 CZ ARG A 8 −19.479 44.080 3.453 1.00 18.56 C ATOM 16 NH1 ARG A 8 −19.744 44.894 4.472 1.00 16.20 N ATOM 17 NH2 ARG A 8 −18.816 42.959 3.671 1.00 13.17 N ATOM 18 O ARG A 8 −24.639 44.451 −1.605 1.00 11.63 O ATOM 19 N ARG A 9 −22.589 44.386 −2.546 1.00 17.31 N ATOM 20 CA ARG A 9 −23.017 43.667 −3.747 1.00 15.23 C ATOM 21 C ARG A 9 −22.202 42.401 −3.960 1.00 12.13 C ATOM 22 O ARG A 9 −21.048 42.328 −3.554 1.00 15.48 O ATOM 23 CB ARG A 9 −22.851 44.558 −4.984 1.00 20.10 C ATOM 24 CG ARG A 9 −23.745 45.788 −5.019 1.00 21.95 C ATOM 25 CD ARG A 9 −23.339 46.711 −6.167 1.00 29.40 C ATOM 26 NE ARG A 9 −24.116 47.949 −6.182 1.00 31.93 N ATOM 27 CZ ARG A 9 −25.269 48.098 −6.824 1.00 41.04 C ATOM 28 NH1 ARG A 9 −25.782 47.087 −7.507 1.00 25.69 N ATOM 29 NH2 ARG A 9 −25.911 49.259 −6.786 1.00 35.67 N ATOM 30 N THR A 10 −22.815 41.422 −4.621 1.00 13.54 N ATOM 31 CA THR A 10 −22.103 40.220 −5.047 1.00 14.38 C ATOM 32 C THR A 10 −21.025 40.604 −6.058 1.00 21.65 C ATOM 33 O THR A 10 −21.064 41.705 −6.620 1.00 18.22 O ATOM 34 CB THR A 10 −23.056 39.216 −5.709 1.00 14.17 C ATOM 35 OG1 THR A 10 −23.504 39.739 −6.972 1.00 14.78 O ATOM 36 CG2 THR A 10 −24.260 38.949 −4.824 1.00 13.27 C ATOM 37 N PRO A 11 −20.050 39.708 −6.288 1.00 18.16 N ATOM 38 CA PRO A 11 −19.002 39.977 −7.280 1.00 20.97 C ATOM 39 C PRO A 11 −19.595 40.202 −8.663 1.00 18.43 C ATOM 40 O PRO A 11 −18.911 40.714 −9.553 1.00 28.22 O ATOM 41 CB PRO A 11 −18.166 38.692 −7.261 1.00 23.08 C ATOM 42 CG PRO A 11 −18.376 38.133 −5.880 1.00 20.36 C ATOM 43 CD PRO A 11 −19.814 38.445 −5.561 1.00 18.78 C ATOM 44 N GLN A 12 −20.857 39.834 −8.837 1.00 16.57 N ATOM 45 CA GLN A 12 −21.559 40.039 −10.095 1.00 20.23 C ATOM 46 C GLN A 12 −22.422 41.311 −10.049 1.00 22.29 C ATOM 47 O GLN A 12 −23.222 41.573 −10.953 1.00 24.66 O ATOM 48 CB GLN A 12 −22.396 38.797 −10.439 1.00 25.03 C ATOM 49 CG GLN A 12 −21.571 37.496 −10.571 1.00 15.70 C ATOM 50 CD GLN A 12 −21.138 36.897 −9.229 1.00 17.63 C ATOM 51 OE1 GLN A 12 −20.084 36.261 −9.130 1.00 21.07 O ATOM 52 NE2 GLN A 12 −21.951 37.096 −8.198 1.00 14.53 N ATOM 53 N SER A 13 −22.250 42.082 −8.974 1.00 21.48 N ATOM 54 CA SER A 13 −22.858 43.409 −8.801 1.00 20.72 C ATOM 55 C SER A 13 −24.332 43.457 −8.369 1.00 23.48 C ATOM 56 O SER A 13 −24.984 44.492 −8.496 1.00 31.32 O ATOM 57 CB SER A 13 −22.605 44.294 −10.028 1.00 28.85 C ATOM 58 OG SER A 13 −21.220 44.583 −10.147 1.00 30.46 O ATOM 59 N ILE A 14 −24.847 42.350 −7.835 1.00 14.51 N ATOM 60 CA AILE A 14 −26.217 42.289 −7.340 0.50 15.83 C ATOM 61 C ILE A 14 −26.235 42.614 −5.846 1.00 16.95 C ATOM 62 O ILE A 14 −25.442 42.063 −5.084 1.00 15.91 O ATOM 63 CB AILE A 14 −26.824 40.881 −7.537 0.50 15.33 C ATOM 64 CG1 AILE A 14 −26.665 40.422 −8.991 0.50 17.26 C ATOM 65 CG2 AILE A 14 −28.283 40.859 −7.120 0.50 16.38 C ATOM 66 CD1 AILE A 14 −27.420 41.277 −9.991 0.50 17.84 C ATOM 67 CA BILE A 14 −26.216 42.309 −7.341 0.50 15.20 C ATOM 68 CB BILE A 14 −26.875 40.935 −7.587 0.50 16.62 C ATOM 69 CG1 BILE A 14 −26.944 40.644 −9.088 0.50 33.69 C ATOM 70 CG2 BILE A 14 −28.261 40.883 −6.973 0.50 19.08 C ATOM 71 CD1 BILE A 14 −27.766 39.427 −9.436 0.50 19.98 C ATOM 72 N PRO A 15 −27.141 43.507 −5.417 1.00 16.97 N ATOM 73 CA PRO A 15 −27.184 43.839 −3.985 1.00 14.74 C ATOM 74 C PRO A 15 −27.555 42.632 −3.125 1.00 12.12 C ATOM 75 O PRO A 15 −28.517 41.925 −3.421 1.00 14.38 O ATOM 76 CB PRO A 15 −28.292 44.898 −3.903 1.00 18.44 C ATOM 77 CG PRO A 15 −28.364 45.482 −5.283 1.00 18.54 C ATOM 78 CD PRO A 15 −28.069 44.335 −6.209 1.00 17.88 C ATOM 79 N TYR A 16 −26.805 42.419 −2.048 1.00 10.96 N ATOM 80 CA TYR A 16 −27.138 41.352 −1.097 1.00 10.67 C ATOM 81 C TYR A 16 −28.503 41.516 −0.436 1.00 12.83 C ATOM 82 O TYR A 16 −29.123 40.536 −0.034 1.00 13.23 O ATOM 83 CB TYR A 16 −26.052 41.183 −0.025 1.00 9.62 C ATOM 84 CG TYR A 16 −24.826 40.476 −0.542 1.00 8.84 C ATOM 85 CD1 TYR A 16 −24.876 39.117 −0.866 1.00 8.85 C ATOM 86 CD2 TYR A 16 −23.633 41.153 −0.724 1.00 8.95 C ATOM 87 CE1 TYR A 16 −23.765 38.465 −1.346 1.00 8.41 C ATOM 88 CE2 TYR A 16 −22.515 40.516 −1.210 1.00 10.20 C ATOM 89 CZ TYR A 16 −22.587 39.168 −1.531 1.00 8.74 C ATOM 90 OH TYR A 16 −21.451 38.558 −2.013 1.00 10.69 O ATOM 91 N GLN A 17 −28.983 42.753 −0.314 1.00 14.18 N ATOM 92 CA GLN A 17 −30.280 42.981 0.326 1.00 17.55 C ATOM 93 C GLN A 17 −31.422 42.262 −0.388 1.00 15.26 C ATOM 94 O GLN A 17 −32.478 42.023 0.195 1.00 23.55 O ATOM 95 CB GLN A 17 −30.581 44.479 0.434 1.00 24.16 C ATOM 96 CG GLN A 17 −30.565 45.205 −0.895 1.00 28.39 C ATOM 97 CD GLN A 17 −30.822 46.694 −0.755 1.00 82.31 C ATOM 98 OE1 GLN A 17 −31.628 47.121 0.072 1.00 39.90 O ATOM 99 NE2 GLN A 17 −30.142 47.492 −1.572 1.00 47.43 N ATOM 100 N ASP A 18 −31.190 41.907 −1.648 1.00 17.60 N ATOM 101 CA ASP A 18 −32.195 41.258 −2.480 1.00 23.44 C ATOM 102 C ASP A 18 −32.059 39.734 −2.474 1.00 19.90 C ATOM 103 O ASP A 18 −32.862 39.029 −3.085 1.00 23.24 O ATOM 104 CB ASP A 18 −32.068 41.765 −3.922 1.00 23.94 C ATOM 105 CG ASP A 18 −32.228 43.271 −4.029 1.00 69.17 C ATOM 106 OD1 ASP A 18 −32.980 43.855 −3.221 1.00 35.65 O ATOM 107 OD2 ASP A 18 −31.604 43.873 −4.928 1.00 45.97 O ATOM 108 N LEU A 19 −31.041 39.233 −1.785 1.00 14.53 N ATOM 109 CA LEU A 19 −30.671 37.821 −1.885 1.00 16.13 C ATOM 110 C LEU A 19 −30.589 37.165 −0.516 1.00 14.97 C ATOM 111 O LEU A 19 −30.294 37.835 0.469 1.00 13.14 O ATOM 112 CB LEU A 19 −29.303 37.700 −2.550 1.00 14.55 C ATOM 113 CG LEU A 19 −29.136 38.357 −3.924 1.00 17.35 C ATOM 114 CD1 LEU A 19 −27.694 38.277 −4.394 1.00 16.13 C ATOM 115 CD2 LEU A 19 −30.080 37.710 −4.927 1.00 21.15 C ATOM 116 N PRO A 20 −30.821 35.844 −0.446 1.00 12.60 N ATOM 117 CA PRO A 20 −30.533 35.158 0.818 1.00 9.83 C ATOM 118 C PRO A 20 −29.035 35.204 1.093 1.00 10.92 C ATOM 119 O PRO A 20 −28.221 34.932 0.209 1.00 10.00 O ATOM 120 CB PRO A 20 −30.996 33.714 0.551 1.00 12.85 C ATOM 121 CG PRO A 20 −31.910 33.798 −0.652 1.00 12.45 C ATOM 122 CD PRO A 20 −31.355 34.929 −1.471 1.00 13.91 C ATOM 123 N HIS A 21 −28.659 35.564 2.315 1.00 9.52 N ATOM 124 CA HIS A 21 −27.255 35.688 2.652 1.00 8.77 C ATOM 125 C HIS A 21 −27.013 35.531 4.145 1.00 8.21 C ATOM 126 O HIS A 21 −27.963 35.527 4.940 1.00 11.76 O ATOM 127 CB HIS A 21 −26.707 37.044 2.193 1.00 12.50 C ATOM 128 CG HIS A 21 −27.346 38.212 2.880 1.00 12.08 C ATOM 129 ND1 HIS A 21 −28.470 38.836 2.386 1.00 17.03 N ATOM 130 CD2 HIS A 21 −27.033 38.852 4.032 1.00 18.83 C ATOM 131 CE1 HIS A 21 −28.819 39.819 3.200 1.00 26.65 C ATOM 132 NE2 HIS A 21 −27.966 39.847 4.206 1.00 21.10 N ATOM 133 N LEU A 22 −25.747 35.406 4.502 1.00 8.64 N ATOM 134 CA LEU A 22 −25.311 35.446 5.895 1.00 6.76 C ATOM 135 C LEU A 22 −23.982 36.170 5.920 1.00 9.47 C ATOM 136 O LEU A 22 −23.294 36.247 4.898 1.00 14.08 O ATOM 137 CB LEU A 22 −25.178 34.038 6.483 1.00 13.24 C ATOM 138 CG LEU A 22 −24.073 33.100 6.000 1.00 15.59 C ATOM 139 CD1 LEU A 22 −22.694 33.547 6.456 1.00 17.18 C ATOM 140 CD2 LEU A 22 −24.349 31.688 6.516 1.00 20.78 C ATOM 141 N VAL A 23 −23.620 36.746 7.058 1.00 6.83 N ATOM 142 CA VAL A 23 −22.341 37.409 7.176 1.00 6.32 C ATOM 143 C VAL A 23 −21.464 36.555 8.079 1.00 6.79 C ATOM 144 O VAL A 23 −21.885 36.200 9.196 1.00 7.54 O ATOM 145 CB VAL A 23 −22.500 38.837 7.772 1.00 7.74 C ATOM 146 CG1 VAL A 23 −21.163 39.562 7.798 1.00 10.24 C ATOM 147 CG2 VAL A 23 −23.538 39.638 6.977 1.00 9.52 C ATOM 148 N ASN A 24 −20.288 36.172 7.603 1.00 6.28 N ATOM 149 CA ASN A 24 −19.422 35.309 8.392 1.00 7.25 C ATOM 150 C ASN A 24 −18.643 36.082 9.467 1.00 8.55 C ATOM 151 O ASN A 24 −18.799 37.308 9.611 1.00 10.11 O ATOM 152 CB ASN A 24 −18.509 34.447 7.496 1.00 6.73 C ATOM 153 CG ASN A 24 −17.357 35.219 6.885 1.00 8.40 C ATOM 154 OD1 ASN A 24 −17.116 36.389 7.213 1.00 8.49 O ATOM 155 ND2 ASN A 24 −16.601 34.553 6.007 1.00 8.52 N ATOM 156 N ALA A 25 −17.824 35.369 10.233 1.00 8.14 N ATOM 157 CA ALA A 25 −17.137 35.971 11.376 1.00 8.35 C ATOM 158 C ALA A 25 −16.101 37.007 10.966 1.00 11.92 C ATOM 159 O ALA A 25 −15.619 37.777 11.803 1.00 15.43 O ATOM 160 CB ALA A 25 −16.497 34.897 12.238 1.00 12.36 C ATOM 161 N ASP A 26 −15.737 37.019 9.687 1.00 10.81 N ATOM 162 CA ASP A 26 −14.794 37.998 9.162 1.00 11.24 C ATOM 163 C ASP A 26 −15.527 39.170 8.504 1.00 9.54 C ATOM 164 O ASP A 26 −14.896 40.025 7.867 1.00 15.54 O ATOM 165 CB ASP A 26 −13.840 37.328 8.166 1.00 11.66 C ATOM 166 CG ASP A 26 −12.891 36.357 8.840 1.00 22.26 C ATOM 167 OD1 ASP A 26 −12.372 36.694 9.930 1.00 24.50 O ATOM 168 OD2 ASP A 26 −12.657 35.258 8.288 1.00 19.65 O ATOM 169 N GLY A 27 −16.847 39.201 8.644 1.00 8.36 N ATOM 170 CA GLY A 27 −17.647 40.275 8.091 1.00 10.32 C ATOM 171 C GLY A 27 −17.901 40.175 6.598 1.00 12.61 C ATOM 172 O GLY A 27 −18.324 41.148 5.976 1.00 12.32 O ATOM 173 N GLN A 28 −17.661 38.998 6.021 1.00 9.34 N ATOM 174 CA GLN A 28 −17.881 38.776 4.588 1.00 8.07 C ATOM 175 C GLN A 28 −19.263 38.219 4.330 1.00 6.30 C ATOM 176 O GLN A 28 −19.725 37.332 5.051 1.00 8.36 O ATOM 177 CB GLN A 28 −16.833 37.810 4.037 1.00 9.11 C ATOM 178 CG GLN A 28 −15.413 38.318 4.197 1.00 10.98 C ATOM 179 CD GLN A 28 −14.370 37.258 3.910 1.00 11.09 C ATOM 180 OE1 GLN A 28 −13.533 37.414 3.005 1.00 15.32 O ATOM 181 NE2 GLN A 28 −14.409 36.177 4.668 1.00 8.14 N ATOM 182 N TYR A 29 −19.950 38.742 3.326 1.00 6.77 N ATOM 183 CA TYR A 29 −21.250 38.230 2.942 1.00 6.19 C ATOM 184 C TYR A 29 −21.135 36.937 2.139 1.00 6.61 C ATOM 185 O TYR A 29 −20.410 36.886 1.130 1.00 8.93 O ATOM 186 CB TYR A 29 −22.002 39.271 2.106 1.00 9.22 C ATOM 187 CG TYR A 29 −22.628 40.389 2.924 1.00 8.73 C ATOM 188 CD1 TYR A 29 −21.838 41.288 3.634 1.00 10.30 C ATOM 189 CD2 TYR A 29 −23.999 40.536 2.983 1.00 10.59 C ATOM 190 CE1 TYR A 29 −22.413 42.307 4.381 1.00 11.19 C ATOM 191 CE2 TYR A 29 −24.582 41.561 3.725 1.00 10.78 C ATOM 192 CZ TYR A 29 −23.773 42.435 4.413 1.00 8.82 C ATOM 193 OH TYR A 29 −24.344 43.451 5.158 1.00 12.21 O ATOM 194 N LEU A 30 −21.853 35.911 2.585 1.00 6.17 N ATOM 195 CA LEU A 30 −21.936 34.654 1.848 1.00 5.98 C ATOM 196 C LEU A 30 −23.334 34.514 1.280 1.00 7.23 C ATOM 197 O LEU A 30 −24.333 34.704 1.975 1.00 9.08 O ATOM 198 CB LEU A 30 −21.629 33.462 2.760 1.00 8.48 C ATOM 199 CG LEU A 30 −20.300 33.501 3.519 1.00 8.51 C ATOM 200 CD1 LEU A 30 −20.093 32.171 4.263 1.00 11.37 C ATOM 201 CD2 LEU A 30 −19.126 33.807 2.603 1.00 10.67 C ATOM 202 N PHE A 31 −23.418 34.168 −0.003 1.00 6.05 N ATOM 203 CA PHE A 31 −24.692 33.900 −0.642 1.00 6.03 C ATOM 204 C PHE A 31 −25.241 32.543 −0.202 1.00 6.46 C ATOM 205 O PHE A 31 −24.484 31.573 −0.167 1.00 6.52 O ATOM 206 CB PHE A 31 −24.508 33.934 −2.167 1.00 6.59 C ATOM 207 CG PHE A 31 −25.711 33.500 −2.921 1.00 7.69 C ATOM 208 CD1 PHE A 31 −26.739 34.395 −3.200 1.00 10.06 C ATOM 209 CD2 PHE A 31 −25.835 32.185 −3.363 1.00 8.63 C ATOM 210 CE1 PHE A 31 −27.869 33.984 −3.895 1.00 12.38 C ATOM 211 CE2 PHE A 31 −26.955 31.778 −4.049 1.00 10.13 C ATOM 212 CZ PHE A 31 −27.974 32.674 −4.321 1.00 11.21 C ATOM 213 N CYS A 32 −26.527 32.483 0.110 1.00 5.60 N ATOM 214 CA CYS A 32 −27.173 31.252 0.594 1.00 5.42 C ATOM 215 C CYS A 32 −28.256 30.757 −0.343 1.00 7.15 C ATOM 216 O CYS A 32 −28.868 31.533 −1.082 1.00 7.80 O ATOM 217 CB CYS A 32 −27.782 31.476 1.982 1.00 7.97 C ATOM 218 SG CYS A 32 −26.589 31.940 3.264 1.00 9.76 S ATOM 219 N ARG A 33 −28.524 29.455 −0.263 1.00 6.41 N ATOM 220 CA ARG A 33 −29.521 28.801 −1.095 1.00 6.58 C ATOM 221 C ARG A 33 −30.301 27.808 −0.238 1.00 6.95 C ATOM 222 O ARG A 33 −29.699 27.074 0.576 1.00 9.26 O ATOM 223 CB ARG A 33 −28.790 28.056 −2.217 1.00 12.39 C ATOM 224 CG ARG A 33 −29.458 28.057 −3.570 1.00 21.52 C ATOM 225 CD ARG A 33 −28.543 27.396 −4.608 1.00 13.00 C ATOM 226 NE ARG A 33 −27.652 28.315 −5.317 1.00 9.53 N ATOM 227 CZ ARG A 33 −28.037 29.049 −6.361 1.00 8.94 C ATOM 228 NH1 ARG A 33 −29.287 28.978 −6.788 1.00 13.78 N ATOM 229 NH2 ARG A 33 −27.172 29.848 −6.972 1.00 10.48 N ATOM 230 N TYR A 34 −31.619 27.773 −0.405 1.00 8.28 N ATOM 231 CA TYR A 34 −32.485 26.905 0.388 1.00 9.23 C ATOM 232 C TYR A 34 −33.474 26.170 −0.498 1.00 12.77 C ATOM 233 O TYR A 34 −33.998 26.735 −1.466 1.00 12.90 O ATOM 234 CB TYR A 34 −33.270 27.722 1.427 1.00 9.73 C ATOM 235 CG TYR A 34 −32.366 28.475 2.366 1.00 10.63 C ATOM 236 CD1 TYR A 34 −31.785 27.835 3.453 1.00 11.93 C ATOM 237 CD2 TYR A 34 −32.066 29.820 2.157 1.00 10.99 C ATOM 238 CE1 TYR A 34 −30.933 28.511 4.301 1.00 12.94 C ATOM 239 CE2 TYR A 34 −31.212 30.505 3.005 1.00 9.78 C ATOM 240 CZ TYR A 34 −30.651 29.838 4.072 1.00 10.20 C ATOM 241 OH TYR A 34 −29.795 30.492 4.921 1.00 11.98 O ATOM 242 N TRP A 35 −33.742 24.916 −0.154 1.00 10.36 N ATOM 243 CA TRP A 35 −34.792 24.152 −0.817 1.00 10.15 C ATOM 244 C TRP A 35 −35.623 23.508 0.286 1.00 11.14 C ATOM 245 O TRP A 35 −35.197 22.524 0.909 1.00 11.77 O ATOM 246 CB TRP A 35 −34.206 23.065 −1.721 1.00 10.42 C ATOM 247 CG TRP A 35 −33.285 23.499 −2.831 1.00 12.61 C ATOM 248 CD1 TRP A 35 −33.609 23.625 −4.160 1.00 13.17 C ATOM 249 CD2 TRP A 35 −31.879 23.777 −2.736 1.00 9.72 C ATOM 250 NE1 TRP A 35 −32.500 23.988 −4.884 1.00 13.29 N ATOM 251 CE2 TRP A 35 −31.421 24.082 −4.041 1.00 11.08 C ATOM 252 CE3 TRP A 35 −30.959 23.791 −1.677 1.00 9.17 C ATOM 253 CZ2 TRP A 35 −30.091 24.403 −4.310 1.00 11.75 C ATOM 254 CZ3 TRP A 35 −29.643 24.108 −1.943 1.00 9.91 C ATOM 255 CH2 TRP A 35 −29.218 24.414 −3.254 1.00 12.71 C ATOM 256 N ALA A 36 −36.793 24.077 0.554 1.00 13.64 N ATOM 257 CA ALA A 36 −37.613 23.643 1.682 1.00 14.33 C ATOM 258 C ALA A 36 −38.871 22.927 1.209 1.00 17.02 C ATOM 259 CB ALA A 36 −37.990 24.850 2.559 1.00 16.53 C ATOM 260 O ALA A 36 −39.523 23.383 0.274 1.00 19.88 O ATOM 261 N PRO A 37 −39.221 21.807 1.859 1.00 14.84 N ATOM 262 CA PRO A 37 −40.460 21.101 1.510 1.00 20.24 C ATOM 263 C PRO A 37 −41.685 21.874 2.015 1.00 18.75 C ATOM 264 O PRO A 37 −41.540 22.811 2.801 1.00 20.85 O ATOM 265 CB PRO A 37 −40.315 19.769 2.257 1.00 19.92 C ATOM 266 CG PRO A 37 −39.457 20.111 3.431 1.00 20.70 C ATOM 267 CD PRO A 37 −38.444 21.075 2.875 1.00 14.82 C ATOM 268 N THR A 38 −42.872 21.479 1.572 1.00 25.39 N ATOM 269 CA THR A 38 −44.096 22.193 1.923 1.00 30.82 C ATOM 270 C THR A 38 −44.415 22.120 3.413 1.00 36.92 C ATOM 271 O THR A 38 −44.878 23.097 4.002 1.00 62.88 O ATOM 272 CB THR A 38 −45.298 21.661 1.127 1.00 40.57 C ATOM 273 OG1 THR A 38 −45.516 20.283 1.455 1.00 75.45 O ATOM 274 CG2 THR A 38 −45.039 21.786 −0.365 1.00 33.30 C ATOM 275 N GLY A 39 −44.169 20.963 4.019 1.00 26.40 N ATOM 276 CA GLY A 39 −44.489 20.769 5.423 1.00 34.27 C ATOM 277 C GLY A 39 −43.270 20.683 6.320 1.00 44.58 C ATOM 278 O GLY A 39 −42.160 21.033 5.914 1.00 35.00 O ATOM 279 N THR A 40 −43.481 20.224 7.550 1.00 28.10 N ATOM 280 CA THR A 40 −42.392 20.033 8.500 1.00 24.60 C ATOM 281 C THR A 40 −41.346 19.088 7.915 1.00 26.04 C ATOM 282 O THR A 40 −41.672 17.976 7.501 1.00 22.08 O ATOM 283 CB THR A 40 −42.902 19.444 9.829 1.00 30.60 C ATOM 284 OG1 THR A 40 −43.947 20.276 10.349 1.00 44.32 O ATOM 285 CG2 THR A 40 −41.772 19.352 10.852 1.00 25.32 C ATOM 286 N PRO A 41 −40.083 19.532 7.871 1.00 20.06 N ATOM 287 CA PRO A 41 −39.027 18.659 7.350 1.00 14.83 C ATOM 288 C PRO A 41 −38.722 17.536 8.332 1.00 15.43 C ATOM 289 O PRO A 41 −38.907 17.706 9.542 1.00 18.25 O ATOM 290 CB PRO A 41 −37.807 19.590 7.246 1.00 15.58 C ATOM 291 CG PRO A 41 −38.331 20.986 7.462 1.00 21.18 C ATOM 292 CD PRO A 41 −39.568 20.847 8.283 1.00 20.08 C ATOM 293 N LYS A 42 −38.244 16.407 7.817 1.00 12.49 N ATOM 294 CA LYS A 42 −37.840 15.276 8.648 1.00 15.17 C ATOM 295 C LYS A 42 −36.405 15.425 9.127 1.00 13.51 C ATOM 296 O LYS A 42 −36.002 14.831 10.133 1.00 15.33 O ATOM 297 CB LYS A 42 −37.978 13.968 7.866 1.00 20.90 C ATOM 298 CG LYS A 42 −39.415 13.620 7.520 1.00 33.71 C ATOM 299 CD LYS A 42 −39.587 12.137 7.262 1.00 65.22 C ATOM 300 CE LYS A 42 −38.819 11.702 6.034 1.00 53.35 C ATOM 301 NZ LYS A 42 −39.110 10.284 5.687 1.00 78.02 N ATOM 302 N ALA A 43 −35.630 16.213 8.387 1.00 11.61 N ATOM 303 CA ALA A 43 −34.228 16.414 8.693 1.00 9.88 C ATOM 304 C ALA A 43 −33.707 17.595 7.880 1.00 7.84 C ATOM 305 O ALA A 43 −34.377 18.073 6.961 1.00 9.50 O ATOM 306 CB ALA A 43 −33.421 15.156 8.373 1.00 13.77 C ATOM 307 N LEU A 44 −32.517 18.047 8.250 1.00 8.06 N ATOM 308 CA LEU A 44 −31.815 19.114 7.551 1.00 7.73 C ATOM 309 C LEU A 44 −30.613 18.507 6.858 1.00 7.26 C ATOM 310 O LEU A 44 −30.001 17.577 7.379 1.00 8.67 O ATOM 311 CB LEU A 44 −31.312 20.154 8.560 1.00 10.75 C ATOM 312 CG LEU A 44 −32.320 20.734 9.558 1.00 14.46 C ATOM 313 CD1 LEU A 44 −31.600 21.580 10.594 1.00 18.22 C ATOM 314 CD2 LEU A 44 −33.367 21.546 8.837 1.00 14.89 C ATOM 315 N ILE A 45 −30.232 19.069 5.718 1.00 7.30 N ATOM 316 CA ILE A 45 −28.991 18.659 5.084 1.00 7.17 C ATOM 317 C ILE A 45 −28.270 19.843 4.445 1.00 6.26 C ATOM 318 O ILE A 45 −28.850 20.592 3.644 1.00 7.44 O ATOM 319 CB ILE A 45 −29.206 17.489 4.079 1.00 7.19 C ATOM 320 CG1 ILE A 45 −27.868 16.995 3.511 1.00 7.97 C ATOM 321 CG2 ILE A 45 −30.224 17.865 3.008 1.00 9.73 C ATOM 322 CD1 ILE A 45 −27.975 15.599 2.857 1.00 11.27 C ATOM 323 N PHE A 46 −27.021 20.011 4.837 1.00 5.88 N ATOM 324 CA PHE A 46 −26.169 21.039 4.251 1.00 5.70 C ATOM 325 C PHE A 46 −25.371 20.481 3.084 1.00 5.52 C ATOM 326 O PHE A 46 −24.738 19.426 3.211 1.00 7.72 O ATOM 327 CB PHE A 46 −25.216 21.629 5.298 1.00 5.92 C ATOM 328 CG PHE A 46 −24.325 22.708 4.757 1.00 6.50 C ATOM 329 CD1 PHE A 46 −23.082 22.413 4.216 1.00 7.76 C ATOM 330 CD2 PHE A 46 −24.758 24.027 4.769 1.00 7.33 C ATOM 331 CE1 PHE A 46 −22.267 23.423 3.693 1.00 7.27 C ATOM 332 CE2 PHE A 46 −23.954 25.038 4.250 1.00 8.02 C ATOM 333 CZ PHE A 46 −22.715 24.742 3.711 1.00 8.11 C ATOM 334 N VAL A 47 −25.375 21.211 1.970 1.00 5.46 N ATOM 335 CA VAL A 47 −24.617 20.813 0.783 1.00 6.17 C ATOM 336 C VAL A 47 −23.379 21.693 0.648 1.00 7.61 C ATOM 337 O VAL A 47 −23.491 22.930 0.600 1.00 8.01 O ATOM 338 CB VAL A 47 −25.480 20.904 −0.495 1.00 9.99 C ATOM 339 CG1 VAL A 47 −24.642 20.584 −1.753 1.00 10.76 C ATOM 340 CG2 VAL A 47 −26.673 19.965 −0.389 1.00 9.71 C ATOM 341 N SER A 48 −22.210 21.053 0.604 1.00 5.98 N ATOM 342 CA SER A 48 −20.915 21.711 0.581 1.00 6.93 C ATOM 343 C SER A 48 −20.251 21.506 −0.791 1.00 7.30 C ATOM 344 O SER A 48 −19.782 20.401 −1.130 1.00 6.87 O ATOM 345 CB SER A 48 −20.035 21.111 1.688 1.00 8.37 C ATOM 346 OG SER A 48 −18.758 21.704 1.745 1.00 8.59 O ATOM 347 N HIS A 49 −20.194 22.579 −1.580 1.00 5.91 N ATOM 348 CA HIS A 49 −19.621 22.526 −2.923 1.00 5.97 C ATOM 349 C HIS A 49 −18.089 22.530 −2.893 1.00 5.83 C ATOM 350 O HIS A 49 −17.461 22.768 −1.861 1.00 5.76 O ATOM 351 CB HIS A 49 −20.161 23.674 −3.800 1.00 6.87 C ATOM 352 CG HIS A 49 −19.608 25.028 −3.457 1.00 4.44 C ATOM 353 ND1 HIS A 49 −18.365 25.450 −3.876 1.00 5.38 N ATOM 354 CD2 HIS A 49 −20.152 26.072 −2.781 1.00 6.37 C ATOM 355 CE1 HIS A 49 −18.151 26.685 −3.445 1.00 7.05 C ATOM 356 NE2 HIS A 49 −19.224 27.087 −2.786 1.00 5.73 N ATOM 357 N GLY A 50 −17.475 22.238 −4.039 1.00 6.83 N ATOM 358 CA GLY A 50 −16.033 22.155 −4.121 1.00 6.75 C ATOM 359 C GLY A 50 −15.362 23.413 −4.651 1.00 6.47 C ATOM 360 O GLY A 50 −16.022 24.420 −4.955 1.00 6.59 O ATOM 361 N ALA A 51 −14.050 23.344 −4.781 1.00 5.98 N ATOM 362 CA ALA A 51 −13.268 24.487 −5.244 1.00 5.62 C ATOM 363 C ALA A 51 −13.654 24.862 −6.662 1.00 8.12 C ATOM 364 O ALA A 51 −13.866 23.984 −7.511 1.00 7.71 O ATOM 365 CB ALA A 51 −11.805 24.181 −5.188 1.00 8.37 C ATOM 366 N GLY A 52 −13.719 26.164 −6.927 1.00 6.60 N ATOM 367 CA GLY A 52 −13.966 26.656 −8.270 1.00 9.14 C ATOM 368 C GLY A 52 −15.413 26.649 −8.709 1.00 7.08 C ATOM 369 O GLY A 52 −15.730 27.192 −9.773 1.00 8.55 O ATOM 370 N GLU A 53 −16.302 26.044 −7.927 1.00 5.30 N ATOM 371 CA GLU A 53 −17.719 26.013 −8.276 1.00 6.20 C ATOM 372 C GLU A 53 −18.570 26.767 −7.242 1.00 5.56 C ATOM 373 O GLU A 53 −18.087 27.730 −6.635 1.00 6.90 O ATOM 374 CB GLU A 53 −18.233 24.582 −8.536 1.00 8.29 C ATOM 375 CG GLU A 53 −17.953 23.602 −7.388 1.00 6.83 C ATOM 376 CD GLU A 53 −18.750 22.300 −7.486 1.00 10.34 C ATOM 377 OE1 GLU A 53 −19.440 22.076 −8.496 1.00 10.71 O ATOM 378 OE2 GLU A 53 −18.712 21.494 −6.522 1.00 9.53 O ATOM 379 N HIS A 54 −19.811 26.356 −7.054 1.00 5.72 N ATOM 380 CA HIS A 54 −20.727 27.085 −6.173 1.00 6.19 C ATOM 381 C HIS A 54 −21.987 26.260 −5.929 1.00 5.74 C ATOM 382 O HIS A 54 −22.179 25.207 −6.563 1.00 7.20 O ATOM 383 CB HIS A 54 −21.089 28.443 −6.801 1.00 7.71 C ATOM 384 CG HIS A 54 −21.857 28.312 −8.079 1.00 6.04 C ATOM 385 ND1 HIS A 54 −23.223 28.457 −8.149 1.00 7.69 N ATOM 386 CD2 HIS A 54 −21.445 27.990 −9.332 1.00 6.29 C ATOM 387 CE1 HIS A 54 −23.622 28.253 −9.395 1.00 8.02 C ATOM 388 NE2 HIS A 54 −22.561 27.967 −10.129 1.00 7.68 N ATOM 389 N SER A 55 −22.869 26.749 −5.064 1.00 6.06 N ATOM 390 CA SER A 55 −24.028 25.992 −4.616 1.00 5.79 C ATOM 391 C SER A 55 −25.064 25.729 −5.710 1.00 6.93 C ATOM 392 O SER A 55 −25.864 24.794 −5.609 1.00 8.85 O ATOM 393 CB SER A 55 −24.697 26.711 −3.434 1.00 7.37 C ATOM 394 OG SER A 55 −25.185 27.981 −3.824 1.00 9.12 O ATOM 395 N GLY A 56 −25.093 26.577 −6.736 1.00 7.19 N ATOM 396 CA GLY A 56 −26.086 26.425 −7.789 1.00 9.39 C ATOM 397 C GLY A 56 −25.890 25.189 −8.663 1.00 8.15 C ATOM 398 O GLY A 56 −26.812 24.773 −9.367 1.00 11.61 O ATOM 399 N ARG A 57 −24.706 24.599 −8.591 1.00 7.21 N ATOM 400 CA ARG A 57 −24.409 23.405 −9.371 1.00 8.23 C ATOM 401 C ARG A 57 −25.023 22.147 −8.738 1.00 12.55 C ATOM 402 O ARG A 57 −24.861 21.049 −9.268 1.00 15.41 O ATOM 403 CB ARG A 57 −22.900 23.280 −9.594 1.00 11.50 C ATOM 404 CG ARG A 57 −22.300 24.548 −10.261 1.00 11.08 C ATOM 405 CD ARG A 57 −21.326 24.258 −11.403 1.00 14.23 C ATOM 406 NE ARG A 57 −21.863 23.251 −12.312 1.00 16.18 N ATOM 407 CZ ARG A 57 −22.803 23.478 −13.219 1.00 20.13 C ATOM 408 NH1 ARG A 57 −23.305 24.698 −13.381 1.00 23.25 N ATOM 409 NH2 ARG A 57 −23.241 22.477 −13.971 1.00 20.33 N ATOM 410 N TYR A 58 −25.759 22.318 −7.639 1.00 8.94 N ATOM 411 CA TYR A 58 −26.351 21.196 −6.889 1.00 8.78 C ATOM 412 C TYR A 58 −27.876 21.187 −6.952 1.00 10.23 C ATOM 413 O TYR A 58 −28.545 20.471 −6.201 1.00 10.07 O ATOM 414 CB TYR A 58 −25.808 21.182 −5.437 1.00 10.33 C ATOM 415 CG TYR A 58 −24.356 20.813 −5.471 1.00 7.86 C ATOM 416 CD1 TYR A 58 −23.367 21.764 −5.755 1.00 8.45 C ATOM 417 CD2 TYR A 58 −23.968 19.487 −5.324 1.00 9.90 C ATOM 418 CE1 TYR A 58 −22.039 21.403 −5.859 1.00 8.11 C ATOM 419 CE2 TYR A 58 −22.649 19.117 −5.413 1.00 8.69 C ATOM 420 CZ TYR A 58 −21.682 20.061 −5.696 1.00 9.51 C ATOM 421 OH TYR A 58 −20.374 19.682 −5.811 1.00 12.95 O ATOM 422 N GLU A 59 −28.429 21.975 −7.869 1.00 9.80 N ATOM 423 CA GLU A 59 −29.868 22.136 −7.978 1.00 11.59 C ATOM 424 C GLU A 59 −30.645 20.816 −8.039 1.00 10.87 C ATOM 425 O GLU A 59 −31.608 20.616 −7.297 1.00 10.96 O ATOM 426 CB GLU A 59 −30.203 22.987 −9.208 1.00 13.77 C ATOM 427 CG GLU A 59 −31.654 23.394 −9.288 1.00 14.77 C ATOM 428 CD GLU A 59 −32.069 24.310 −8.144 1.00 16.52 C ATOM 429 OE1 GLU A 59 −31.216 25.088 −7.671 1.00 20.67 O ATOM 430 OE2 GLU A 59 −33.245 24.251 −7.728 1.00 25.13 O ATOM 431 N GLU A 60 −30.235 19.916 −8.930 1.00 10.53 N ATOM 432 CA GLU A 60 −30.993 18.683 −9.117 1.00 10.68 C ATOM 433 C GLU A 60 −30.896 17.758 −7.908 1.00 9.92 C ATOM 434 O GLU A 60 −31.894 17.181 −7.476 1.00 10.77 O ATOM 435 CB GLU A 60 −30.553 17.959 −10.391 1.00 14.50 C ATOM 436 CG GLU A 60 −30.925 18.708 −11.667 1.00 24.44 C ATOM 437 CD GLU A 60 −32.401 19.063 −11.722 1.00 89.95 C ATOM 438 OE1 GLU A 60 −33.241 18.168 −11.485 1.00 55.36 O ATOM 439 OE2 GLU A 60 −32.723 20.237 −12.003 1.00 106.69 O ATOM 440 N LEU A 61 −29.694 17.608 −7.372 1.00 8.91 N ATOM 441 CA ALEU A 61 −29.506 16.811 −6.161 0.50 9.95 C ATOM 442 C LEU A 61 −30.339 17.376 −5.013 1.00 10.94 C ATOM 443 O LEU A 61 −31.003 16.637 −4.278 1.00 9.90 O ATOM 444 CB ALEU A 61 −28.031 16.777 −5.757 0.50 11.94 C ATOM 445 CG ALEU A 61 −27.140 15.693 −6.367 0.50 9.56 C ATOM 446 CD1 ALEU A 61 −25.700 15.937 −5.975 0.50 8.30 C ATOM 447 CD2 ALEU A 61 −27.591 14.303 −5.926 0.50 9.49 C ATOM 448 CA BLEU A 61 −29.513 16.807 −6.168 0.50 9.77 C ATOM 449 CB BLEU A 61 −28.039 16.757 −5.782 0.50 12.63 C ATOM 450 CG BLEU A 61 −27.659 15.622 −4.834 0.50 14.96 C ATOM 451 CD1 BLEU A 61 −28.276 14.307 −5.303 0.50 15.85 C ATOM 452 CD2 BLEU A 61 −26.151 15.511 −4.742 0.50 14.56 C ATOM 453 N ALA A 62 −30.303 18.694 −4.849 1.00 8.48 N ATOM 454 CA ALA A 62 −31.054 19.331 −3.778 1.00 10.11 C ATOM 455 C ALA A 62 −32.555 19.111 −3.938 1.00 13.13 C ATOM 456 O ALA A 62 −33.267 18.881 −2.955 1.00 10.27 O ATOM 457 CB ALA A 62 −30.732 20.826 −3.722 1.00 10.95 C ATOM 458 N ARG A 63 −33.052 19.194 −5.169 1.00 9.46 N ATOM 459 CA ARG A 63 −34.475 18.973 −5.402 1.00 13.75 C ATOM 460 C ARG A 63 −34.891 17.549 −5.042 1.00 11.63 C ATOM 461 O ARG A 63 −35.964 17.327 −4.481 1.00 12.65 O ATOM 462 CB ARG A 63 −34.846 19.301 −6.849 1.00 11.63 C ATOM 463 CG ARG A 63 −34.838 20.793 −7.131 1.00 15.77 C ATOM 464 CD ARG A 63 −35.202 21.085 −8.579 1.00 27.72 C ATOM 465 NE ARG A 63 −35.167 22.516 −8.871 1.00 33.09 N ATOM 466 CZ ARG A 63 −35.623 23.058 −9.995 1.00 84.41 C ATOM 467 NH1 ARG A 63 −36.156 22.291 −10.937 1.00 43.78 N ATOM 468 NH2 ARG A 63 −35.549 24.370 −10.175 1.00 46.62 N ATOM 469 N MET A 64 −34.035 16.584 −5.362 1.00 10.52 N ATOM 470 CA AMET A 64 −34.299 15.192 −5.002 0.75 11.44 C ATOM 471 C MET A 64 −34.394 15.041 −3.485 1.00 11.99 C ATOM 472 O MET A 64 −35.315 14.410 −2.965 1.00 12.08 O ATOM 473 CB AMET A 64 −33.212 14.277 −5.575 0.75 11.53 C ATOM 474 CG AMET A 64 −33.399 12.800 −5.229 0.75 11.45 C ATOM 475 SD AMET A 64 −32.651 12.319 −3.663 0.75 14.16 S ATOM 476 CE AMET A 64 −30.923 12.298 −4.124 0.75 13.84 C ATOM 477 CA BMET A 64 −34.318 15.202 −5.003 0.25 12.08 C ATOM 478 CB BMET A 64 −33.259 14.270 −5.583 0.25 12.80 C ATOM 479 CG BMET A 64 −33.680 12.815 −5.583 0.25 26.52 C ATOM 480 SD BMET A 64 −32.270 11.723 −5.382 0.25 12.18 S ATOM 481 CE BMET A 64 −31.712 12.205 −3.742 0.25 0.00 C ATOM 482 N LEU A 65 −33.437 15.628 −2.777 1.00 9.40 N ATOM 483 CA LEU A 65 −33.394 15.534 −1.319 1.00 10.14 C ATOM 484 C LEU A 65 −34.594 16.228 −0.671 1.00 10.86 C ATOM 485 O LEU A 65 −35.174 15.723 0.296 1.00 10.56 O ATOM 486 CB LEU A 65 −32.082 16.117 −0.793 1.00 8.51 C ATOM 487 CG LEU A 65 −30.836 15.282 −1.120 1.00 10.20 C ATOM 488 CD1 LEU A 65 −29.562 16.095 −0.943 1.00 11.61 C ATOM 489 CD2 LEU A 65 −30.803 14.004 −0.274 1.00 12.05 C ATOM 490 N MET A 66 −34.973 17.383 −1.209 1.00 11.05 N ATOM 491 CA AMET A 66 −36.136 18.088 −0.703 0.50 11.92 C ATOM 492 C MET A 66 −37.395 17.241 −0.931 1.00 14.01 C ATOM 493 O MET A 66 −38.328 17.265 −0.120 1.00 14.48 O ATOM 494 CB AMET A 66 −36.239 19.471 −1.354 0.50 7.66 C ATOM 495 CG AMET A 66 −37.413 20.298 −0.867 0.50 16.42 C ATOM 496 SD AMET A 66 −38.927 19.913 −1.763 0.50 19.91 S ATOM 497 CE AMET A 66 −38.623 20.747 −3.320 0.50 29.87 C ATOM 498 CA BMET A 66 −36.151 18.103 −0.735 0.50 10.75 C ATOM 499 CB BMET A 66 −36.301 19.432 −1.483 0.50 20.22 C ATOM 500 CG BMET A 66 −37.520 20.250 −1.071 0.50 16.81 C ATOM 501 SD BMET A 66 −37.739 21.751 −2.054 0.50 18.63 S ATOM 502 CE BMET A 66 −38.028 21.070 −3.685 0.50 28.73 C ATOM 503 N GLY A 67 −37.404 16.473 −2.021 1.00 12.11 N ATOM 504 CA GLY A 67 −38.501 15.567 −2.320 1.00 18.68 C ATOM 505 C GLY A 67 −38.616 14.423 −1.324 1.00 13.55 C ATOM 506 O GLY A 67 −39.651 13.763 −1.249 1.00 17.32 O ATOM 507 N LEU A 68 −37.550 14.180 −0.570 1.00 14.11 N ATOM 508 CA LEU A 68 −37.555 13.207 0.520 1.00 15.51 C ATOM 509 C LEU A 68 −37.984 13.857 1.838 1.00 15.63 C ATOM 510 O LEU A 68 −37.854 13.257 2.911 1.00 17.55 O ATOM 511 CB LEU A 68 −36.164 12.605 0.693 1.00 14.48 C ATOM 512 CG LEU A 68 −35.579 11.827 −0.482 1.00 16.34 C ATOM 513 CD1 LEU A 68 −34.187 11.326 −0.122 1.00 19.31 C ATOM 514 CD2 LEU A 68 −36.495 10.672 −0.866 1.00 25.16 C ATOM 515 N ASP A 69 −38.477 15.090 1.742 1.00 15.49 N ATOM 516 CA ASP A 69 −38.936 15.859 2.903 1.00 13.48 C ATOM 517 C ASP A 69 −37.799 16.365 3.800 1.00 14.51 C ATOM 518 O ASP A 69 −37.982 16.554 5.007 1.00 15.76 O ATOM 519 CB ASP A 69 −39.958 15.059 3.724 1.00 18.23 C ATOM 520 CG ASP A 69 −40.801 15.939 4.622 1.00 52.91 C ATOM 521 OD1 ASP A 69 −41.032 17.110 4.255 1.00 35.35 O ATOM 522 OD2 ASP A 69 −41.236 15.461 5.690 1.00 43.13 O ATOM 523 N LEU A 70 −36.622 16.574 3.219 1.00 11.72 N ATOM 524 CA LEU A 70 −35.529 17.218 3.940 1.00 12.54 C ATOM 525 C LEU A 70 −35.487 18.700 3.571 1.00 11.28 C ATOM 526 O LEU A 70 −35.809 19.083 2.444 1.00 12.36 O ATOM 527 CB LEU A 70 −34.174 16.572 3.621 1.00 12.49 C ATOM 528 CG LEU A 70 −33.854 15.265 4.351 1.00 19.34 C ATOM 529 CD1 LEU A 70 −34.549 14.111 3.654 1.00 21.20 C ATOM 530 CD2 LEU A 70 −32.350 15.016 4.415 1.00 16.83 C ATOM 531 N LEU A 71 −35.100 19.533 4.530 1.00 9.16 N ATOM 532 CA LEU A 71 −34.777 20.916 4.226 1.00 9.27 C ATOM 533 C LEU A 71 −33.307 20.979 3.834 1.00 8.70 C ATOM 534 O LEU A 71 −32.415 20.689 4.639 1.00 8.84 O ATOM 535 CB LEU A 71 −35.051 21.799 5.440 1.00 10.92 C ATOM 536 CG LEU A 71 −35.014 23.311 5.176 1.00 14.41 C ATOM 537 CD1 LEU A 71 −35.732 24.045 6.305 1.00 17.57 C ATOM 538 CD2 LEU A 71 −33.592 23.831 5.014 1.00 17.60 C ATOM 539 N VAL A 72 −33.060 21.347 2.586 1.00 7.86 N ATOM 540 CA VAL A 72 −31.708 21.395 2.055 1.00 8.85 C ATOM 541 C VAL A 72 −31.214 22.828 2.109 1.00 8.92 C ATOM 542 O VAL A 72 −31.950 23.753 1.749 1.00 7.86 O ATOM 543 CB VAL A 72 −31.668 20.911 0.591 1.00 7.35 C ATOM 544 CG1 VAL A 72 −30.227 20.797 0.097 1.00 9.49 C ATOM 545 CG2 VAL A 72 −32.412 19.583 0.451 1.00 9.13 C ATOM 546 N PHE A 73 −29.986 23.021 2.561 1.00 6.35 N ATOM 547 CA PHE A 73 −29.439 24.374 2.612 1.00 6.13 C ATOM 548 C PHE A 73 −27.967 24.386 2.237 1.00 7.10 C ATOM 549 O PHE A 73 −27.275 23.372 2.342 1.00 6.36 O ATOM 550 CB PHE A 73 −29.728 25.081 3.959 1.00 6.94 C ATOM 551 CG PHE A 73 −29.071 24.458 5.160 1.00 7.16 C ATOM 552 CD1 PHE A 73 −29.459 23.209 5.624 1.00 8.74 C ATOM 553 CD2 PHE A 73 −28.101 25.156 5.873 1.00 9.73 C ATOM 554 CE1 PHE A 73 −28.858 22.649 6.746 1.00 11.57 C ATOM 555 CE2 PHE A 73 −27.503 24.609 7.010 1.00 11.39 C ATOM 556 CZ PHE A 73 −27.889 23.356 7.450 1.00 11.64 C ATOM 557 N ALA A 74 −27.487 25.535 1.771 1.00 5.58 N ATOM 558 CA ALA A 74 −26.122 25.665 1.312 1.00 6.13 C ATOM 559 C ALA A 74 −25.710 27.124 1.322 1.00 5.53 C ATOM 560 O ALA A 74 −26.562 28.008 1.381 1.00 5.91 O ATOM 561 CB ALA A 74 −25.996 25.112 −0.117 1.00 7.97 C ATOM 562 N HIS A 75 −24.418 27.365 1.229 1.00 5.08 N ATOM 563 CA HIS A 75 −23.942 28.683 0.855 1.00 4.98 C ATOM 564 C HIS A 75 −22.762 28.529 −0.070 1.00 6.30 C ATOM 565 O HIS A 75 −22.151 27.455 −0.160 1.00 6.97 O ATOM 566 CB HIS A 75 −23.603 29.556 2.073 1.00 5.32 C ATOM 567 CG HIS A 75 −22.565 28.985 2.985 1.00 6.21 C ATOM 568 ND1 HIS A 75 −22.865 28.561 4.263 1.00 7.36 N ATOM 569 CD2 HIS A 75 −21.228 28.821 2.835 1.00 6.89 C ATOM 570 CE1 HIS A 75 −21.758 28.146 4.854 1.00 6.18 C ATOM 571 NE2 HIS A 75 −20.747 28.289 4.012 1.00 6.86 N ATOM 572 N ASP A 76 −22.428 29.608 −0.771 1.00 5.01 N ATOM 573 CA ASP A 76 −21.200 29.646 −1.548 1.00 5.14 C ATOM 574 C ASP A 76 −20.058 29.931 −0.589 1.00 5.33 C ATOM 575 O ASP A 76 −20.124 30.898 0.189 1.00 5.80 O ATOM 576 CB ASP A 76 −21.280 30.708 −2.658 1.00 6.05 C ATOM 577 CG ASP A 76 −22.301 30.360 −3.726 1.00 7.92 C ATOM 578 OD1 ASP A 76 −22.795 29.212 −3.750 1.00 7.77 O ATOM 579 OD2 ASP A 76 −22.637 31.243 −4.548 1.00 7.72 O ATOM 580 N HIS A 77 −19.043 29.077 −0.577 1.00 5.59 N ATOM 581 CA HIS A 77 −17.908 29.282 0.298 1.00 5.52 C ATOM 582 C HIS A 77 −17.261 30.624 −0.020 1.00 5.25 C ATOM 583 O HIS A 77 −17.368 31.144 −1.141 1.00 6.90 O ATOM 584 CB HIS A 77 −16.872 28.166 0.122 1.00 7.14 C ATOM 585 CG HIS A 77 −17.404 26.795 0.413 1.00 6.26 C ATOM 586 ND1 HIS A 77 −17.922 26.440 1.641 1.00 8.66 N ATOM 587 CD2 HIS A 77 −17.465 25.679 −0.357 1.00 7.29 C ATOM 588 CE1 HIS A 77 −18.313 25.176 1.605 1.00 9.31 C ATOM 589 NE2 HIS A 77 −18.035 24.689 0.407 1.00 9.66 N ATOM 590 N VAL A 78 −16.572 31.196 0.956 1.00 6.80 N ATOM 591 CA AVAL A 78 −15.924 32.466 0.703 0.50 6.73 C ATOM 592 C VAL A 78 −15.026 32.332 −0.531 1.00 7.87 C ATOM 593 CB AVAL A 78 −15.163 32.972 1.947 0.50 15.02 C ATOM 594 CG1 AVAL A 78 −13.972 32.076 2.248 0.50 3.02 C ATOM 595 CG2 AVAL A 78 −14.756 34.438 1.771 0.50 5.54 C ATOM 596 O VAL A 78 −14.417 31.286 −0.791 1.00 7.09 O ATOM 597 CA BVAL A 78 −15.839 32.437 0.752 0.50 10.12 C ATOM 598 CB BVAL A 78 −14.889 32.695 1.942 0.50 4.36 C ATOM 599 CG1 BVAL A 78 −13.801 33.684 1.564 0.50 10.71 C ATOM 600 CG2 BVAL A 78 −15.667 33.180 3.151 0.50 15.80 C ATOM 601 N GLY A 79 −15.002 33.392 −1.338 1.00 7.60 N ATOM 602 CA GLY A 79 −14.198 33.399 −2.552 1.00 8.95 C ATOM 603 C GLY A 79 −14.813 32.627 −3.704 1.00 5.87 C ATOM 604 O GLY A 79 −14.131 32.419 −4.721 1.00 8.58 O ATOM 605 N HIS A 80 −16.072 32.226 −3.569 1.00 4.89 N ATOM 606 CA HIS A 80 −16.745 31.427 −4.592 1.00 4.97 C ATOM 607 C HIS A 80 −18.108 31.959 −4.922 1.00 6.40 C ATOM 608 O HIS A 80 −18.766 32.612 −4.100 1.00 6.52 O ATOM 609 CB HIS A 80 −16.888 29.958 −4.138 1.00 5.51 C ATOM 610 CG HIS A 80 −15.581 29.255 −3.999 1.00 7.26 C ATOM 611 ND1 HIS A 80 −15.113 28.348 −4.931 1.00 9.83 N ATOM 612 CD2 HIS A 80 −14.609 29.374 −3.067 1.00 4.47 C ATOM 613 CE1 HIS A 80 −13.918 27.921 −4.561 1.00 4.41 C ATOM 614 NE2 HIS A 80 −13.591 28.527 −3.431 1.00 11.14 N ATOM 615 N GLY A 81 −18.558 31.659 −6.134 1.00 7.03 N ATOM 616 CA GLY A 81 −19.903 31.969 −6.550 1.00 7.68 C ATOM 617 C GLY A 81 −20.301 33.409 −6.297 1.00 7.61 C ATOM 618 O GLY A 81 −19.609 34.336 −6.722 1.00 8.19 O ATOM 619 N GLN A 82 −21.410 33.585 −5.595 1.00 7.12 N ATOM 620 CA GLN A 82 −21.947 34.916 −5.350 1.00 7.50 C ATOM 621 C GLN A 82 −21.557 35.462 −3.983 1.00 8.34 C ATOM 622 O GLN A 82 −22.111 36.478 −3.553 1.00 9.53 O ATOM 623 CB GLN A 82 −23.459 34.917 −5.510 1.00 7.66 C ATOM 624 CG GLN A 82 −23.918 34.420 −6.890 1.00 7.96 C ATOM 625 CD GLN A 82 −25.416 34.400 −7.029 1.00 11.20 C ATOM 626 OE1 GLN A 82 −26.058 35.446 −7.145 1.00 12.46 O ATOM 627 NE2 GLN A 82 −25.998 33.207 −7.017 1.00 9.37 N ATOM 628 N SER A 83 −20.630 34.787 −3.306 1.00 6.24 N ATOM 629 CA SER A 83 −20.130 35.262 −2.022 1.00 5.93 C ATOM 630 C SER A 83 −18.974 36.210 −2.224 1.00 7.64 C ATOM 631 O SER A 83 −18.346 36.241 −3.292 1.00 9.96 O ATOM 632 CB SER A 83 −19.670 34.088 −1.157 1.00 6.90 C ATOM 633 OG SER A 83 −20.781 33.296 −0.820 1.00 5.65 O ATOM 634 N GLU A 84 −18.684 36.989 −1.185 1.00 8.21 N ATOM 635 CA GLU A 84 −17.549 37.900 −1.200 1.00 8.55 C ATOM 636 C GLU A 84 −16.218 37.169 −1.054 1.00 10.87 C ATOM 637 O GLU A 84 −16.181 35.963 −0.796 1.00 10.07 O ATOM 638 CB GLU A 84 −17.701 38.956 −0.097 1.00 8.81 C ATOM 639 CG GLU A 84 −18.819 39.932 −0.371 1.00 10.32 C ATOM 640 CD GLU A 84 −18.897 41.045 0.662 1.00 14.70 C ATOM 641 OE1 GLU A 84 −18.584 40.792 1.844 1.00 12.02 O ATOM 642 OE2 GLU A 84 −19.285 42.171 0.285 1.00 17.48 O ATOM 643 N GLY A 85 −15.123 37.909 −1.214 1.00 10.41 N ATOM 644 CA GLY A 85 −13.785 37.373 −1.061 1.00 11.16 C ATOM 645 C GLY A 85 −13.025 37.311 −2.371 1.00 12.67 C ATOM 646 O GLY A 85 −13.611 37.083 −3.428 1.00 12.70 O ATOM 647 N GLU A 86 −11.717 37.516 −2.307 1.00 12.86 N ATOM 648 CA GLU A 86 −10.900 37.312 −3.497 1.00 15.49 C ATOM 649 C GLU A 86 −11.139 35.894 −4.012 1.00 14.29 C ATOM 650 O GLU A 86 −11.252 34.955 −3.220 1.00 11.66 O ATOM 651 CB GLU A 86 −9.429 37.536 −3.177 1.00 16.36 C ATOM 652 CG GLU A 86 −9.114 38.976 −2.782 1.00 31.32 C ATOM 653 CD GLU A 86 −7.662 39.174 −2.392 1.00 101.84 C ATOM 654 OE1 GLU A 86 −6.862 38.229 −2.567 1.00 54.48 O ATOM 655 OE2 GLU A 86 −7.321 40.277 −1.912 1.00 74.42 O ATOM 656 N ARG A 87 −11.240 35.739 −5.329 1.00 12.44 N ATOM 657 CA ARG A 87 −11.629 34.455 −5.910 1.00 11.77 C ATOM 658 C ARG A 87 −10.641 33.329 −5.596 1.00 10.94 C ATOM 659 O ARG A 87 −9.435 33.443 −5.846 1.00 11.69 O ATOM 660 CB ARG A 87 −11.803 34.562 −7.432 1.00 12.45 C ATOM 661 CG ARG A 87 −12.817 35.592 −7.926 1.00 17.92 C ATOM 662 CD ARG A 87 −14.243 35.195 −7.585 1.00 18.43 C ATOM 663 NE ARG A 87 −14.578 35.661 −6.249 1.00 11.89 N ATOM 664 CZ ARG A 87 −15.736 35.459 −5.638 1.00 12.44 C ATOM 665 NH1 ARG A 87 −16.707 34.782 −6.235 1.00 13.57 N ATOM 666 NH2 ARG A 87 −15.916 35.950 −4.414 1.00 13.60 N ATOM 667 N MET A 88 −11.172 32.232 −5.059 1.00 9.91 N ATOM 668 CA MET A 88 −10.380 31.028 −4.820 1.00 11.60 C ATOM 669 C MET A 88 −9.109 31.274 −4.009 1.00 12.66 C ATOM 670 O MET A 88 −8.019 30.791 −4.335 1.00 13.08 O ATOM 671 CB MET A 88 −10.068 30.294 −6.129 1.00 13.27 C ATOM 672 CG MET A 88 −11.227 29.455 −6.646 1.00 23.14 C ATOM 673 SD MET A 88 −10.720 28.240 −7.892 1.00 20.98 S ATOM 674 CE MET A 88 −9.588 27.226 −6.961 1.00 30.54 C ATOM 675 N VAL A 89 −9.285 32.044 −2.942 1.00 9.61 N ATOM 676 CA AVAL A 89 −8.252 32.187 −1.938 0.50 8.87 C ATOM 677 C VAL A 89 −8.935 32.155 −0.579 1.00 8.58 C ATOM 678 O VAL A 89 −10.128 32.442 −0.452 1.00 10.43 O ATOM 679 CB AVAL A 89 −7.439 33.484 −2.102 0.50 20.29 C ATOM 680 CG1 AVAL A 89 −6.728 33.502 −3.451 0.50 21.26 C ATOM 681 CG2 AVAL A 89 −8.335 34.689 −1.951 0.50 11.60 C ATOM 682 CA BVAL A 89 −8.264 32.316 −1.942 0.50 15.07 C ATOM 683 CB BVAL A 89 −7.752 33.771 −2.069 0.50 13.11 C ATOM 684 CG1 BVAL A 89 −7.120 34.254 −0.767 0.50 15.31 C ATOM 685 CG2 BVAL A 89 −6.786 33.900 −3.241 0.50 28.13 C ATOM 686 N VAL A 90 −8.184 31.737 0.427 1.00 9.08 N ATOM 687 CA VAL A 90 −8.738 31.651 1.774 1.00 11.86 C ATOM 688 C VAL A 90 −7.583 31.817 2.759 1.00 11.67 C ATOM 689 O VAL A 90 −6.506 31.267 2.556 1.00 10.65 O ATOM 690 CB VAL A 90 −9.530 30.322 1.992 1.00 9.75 C ATOM 691 CG1 VAL A 90 −8.584 29.132 2.112 1.00 10.71 C ATOM 692 CG2 VAL A 90 −10.449 30.428 3.209 1.00 12.69 C ATOM 693 N SER A 91 −7.793 32.610 3.807 1.00 11.86 N ATOM 694 CA SER A 91 −6.708 32.895 4.745 1.00 11.26 C ATOM 695 C SER A 91 −6.179 31.607 5.380 1.00 10.82 C ATOM 696 O SER A 91 −4.972 31.401 5.489 1.00 13.74 O ATOM 697 CB SER A 91 −7.170 33.884 5.817 1.00 14.65 C ATOM 698 OG SER A 91 −8.265 33.367 6.549 1.00 16.21 O ATOM 699 N ASP A 92 −7.105 30.743 5.789 1.00 10.07 N ATOM 700 CA ASP A 92 −6.784 29.407 6.285 1.00 9.45 C ATOM 701 C ASP A 92 −7.983 28.523 5.981 1.00 8.51 C ATOM 702 O ASP A 92 −9.130 28.967 6.055 1.00 8.70 O ATOM 703 CB ASP A 92 −6.516 29.407 7.795 1.00 12.63 C ATOM 704 CG ASP A 92 −6.132 28.016 8.322 1.00 12.62 C ATOM 705 OD1 ASP A 92 −4.934 27.663 8.272 1.00 15.77 O ATOM 706 OD2 ASP A 92 −7.030 27.276 8.782 1.00 13.34 O ATOM 707 N PHE A 93 −7.714 27.266 5.644 1.00 7.96 N ATOM 708 CA PHE A 93 −8.783 26.351 5.260 1.00 9.18 C ATOM 709 C PHE A 93 −9.900 26.284 6.304 1.00 7.89 C ATOM 710 O PHE A 93 −11.059 26.057 5.975 1.00 8.19 O ATOM 711 CB PHE A 93 −8.233 24.949 4.997 1.00 8.72 C ATOM 712 CG PHE A 93 −9.171 24.080 4.204 1.00 8.08 C ATOM 713 CD1 PHE A 93 −9.243 24.196 2.822 1.00 9.70 C ATOM 714 CD2 PHE A 93 −9.994 23.163 4.834 1.00 9.05 C ATOM 715 CE1 PHE A 93 −10.117 23.401 2.082 1.00 8.73 C ATOM 716 CE2 PHE A 93 −10.870 22.363 4.105 1.00 9.40 C ATOM 717 CZ PHE A 93 −10.936 22.488 2.726 1.00 8.70 C ATOM 718 N HIS A 94 −9.546 26.468 7.572 1.00 7.76 N ATOM 719 CA HIS A 94 −10.545 26.363 8.621 1.00 9.12 C ATOM 720 C HIS A 94 −11.690 27.367 8.476 1.00 6.64 C ATOM 721 O HIS A 94 −12.782 27.138 8.982 1.00 8.47 O ATOM 722 CB HIS A 94 −9.922 26.487 10.014 1.00 10.83 C ATOM 723 CG HIS A 94 −10.891 26.175 11.107 1.00 12.48 C ATOM 724 ND1 HIS A 94 −11.497 27.153 11.868 1.00 18.24 N ATOM 725 CD2 HIS A 94 −11.407 24.996 11.526 1.00 14.58 C ATOM 726 CE1 HIS A 94 −12.323 26.586 12.729 1.00 18.04 C ATOM 727 NE2 HIS A 94 −12.289 25.278 12.541 1.00 20.93 N ATOM 728 N VAL A 95 −11.433 28.476 7.790 1.00 6.79 N ATOM 729 CA VAL A 95 −12.482 29.445 7.525 1.00 7.84 C ATOM 730 C VAL A 95 −13.713 28.751 6.923 1.00 5.99 C ATOM 731 O VAL A 95 −14.852 29.036 7.299 1.00 7.00 O ATOM 732 CB VAL A 95 −11.981 30.569 6.580 1.00 9.46 C ATOM 733 CG1 VAL A 95 −13.146 31.338 5.972 1.00 10.88 C ATOM 734 CG2 VAL A 95 −11.040 31.504 7.333 1.00 10.22 C ATOM 735 N PHE A 96 −13.482 27.834 5.976 1.00 5.97 N ATOM 736 CA PHE A 96 −14.606 27.148 5.328 1.00 6.34 C ATOM 737 C PHE A 96 −15.432 26.338 6.323 1.00 4.91 C ATOM 738 O PHE A 96 −16.661 26.310 6.262 1.00 6.56 O ATOM 739 CB PHE A 96 −14.124 26.191 4.231 1.00 7.50 C ATOM 740 CG PHE A 96 −13.463 26.855 3.057 1.00 6.47 C ATOM 741 CD1 PHE A 96 −13.997 27.991 2.453 1.00 7.28 C ATOM 742 CD2 PHE A 96 −12.332 26.286 2.512 1.00 7.30 C ATOM 743 CE1 PHE A 96 −13.378 28.572 1.333 1.00 8.59 C ATOM 744 CE2 PHE A 96 −11.707 26.847 1.388 1.00 8.91 C ATOM 745 CZ PHE A 96 −12.237 27.993 0.794 1.00 7.27 C ATOM 746 N VAL A 97 −14.732 25.648 7.228 1.00 6.11 N ATOM 747 CA VAL A 97 −15.375 24.815 8.242 1.00 6.27 C ATOM 748 C VAL A 97 −16.135 25.682 9.259 1.00 5.36 C ATOM 749 O VAL A 97 −17.277 25.403 9.594 1.00 6.07 O ATOM 750 CB VAL A 97 −14.312 23.943 8.952 1.00 7.37 C ATOM 751 CG1 VAL A 97 −14.941 23.145 10.091 1.00 10.36 C ATOM 752 CG2 VAL A 97 −13.620 23.008 7.943 1.00 9.21 C ATOM 753 N ARG A 98 −15.480 26.734 9.740 1.00 6.54 N ATOM 754 CA ARG A 98 −16.117 27.695 10.638 1.00 7.12 C ATOM 755 C ARG A 98 −17.430 28.221 10.051 1.00 5.89 C ATOM 756 O ARG A 98 −18.456 28.299 10.723 1.00 6.29 O ATOM 757 CB ARG A 98 −15.142 28.850 10.852 1.00 8.63 C ATOM 758 CG ARG A 98 −15.637 29.977 11.756 1.00 10.60 C ATOM 759 CD ARG A 98 −14.744 31.189 11.573 1.00 10.59 C ATOM 760 NE ARG A 98 −15.017 31.792 10.268 1.00 10.15 N ATOM 761 CZ ARG A 98 −14.335 32.796 9.731 1.00 10.10 C ATOM 762 NH1 ARG A 98 −13.310 33.337 10.377 1.00 11.94 N ATOM 763 NH2 ARG A 98 −14.697 33.265 8.543 1.00 10.42 N ATOM 764 N ASP A 99 −17.395 28.585 8.770 1.00 6.39 N ATOM 765 CA ASP A 99 −18.579 29.151 8.127 1.00 7.52 C ATOM 766 C ASP A 99 −19.709 28.118 7.947 1.00 4.77 C ATOM 767 O ASP A 99 −20.882 28.438 8.121 1.00 5.81 O ATOM 768 CB ASP A 99 −18.211 29.818 6.795 1.00 7.19 C ATOM 769 CG ASP A 99 −17.358 31.083 6.974 1.00 9.39 C ATOM 770 OD1 ASP A 99 −17.061 31.490 8.129 1.00 9.24 O ATOM 771 OD2 ASP A 99 −16.950 31.677 5.948 1.00 8.90 O ATOM 772 N VAL A 100 −19.349 26.875 7.611 1.00 5.99 N ATOM 773 CA VAL A 100 −20.360 25.815 7.575 1.00 5.66 C ATOM 774 C VAL A 100 −21.017 25.659 8.958 1.00 4.09 C ATOM 775 O VAL A 100 −22.228 25.583 9.061 1.00 6.12 O ATOM 776 CB VAL A 100 −19.783 24.457 7.079 1.00 5.14 C ATOM 777 CG1 VAL A 100 −20.807 23.349 7.288 1.00 8.00 C ATOM 778 CG2 VAL A 100 −19.404 24.560 5.599 1.00 8.22 C ATOM 779 N LEU A 101 −20.184 25.628 10.001 1.00 5.14 N ATOM 780 CA LEU A 101 −20.722 25.484 11.361 1.00 6.56 C ATOM 781 C LEU A 101 −21.636 26.651 11.768 1.00 6.23 C ATOM 782 O LEU A 101 −22.652 26.444 12.419 1.00 6.91 O ATOM 783 CB LEU A 101 −19.591 25.278 12.369 1.00 7.60 C ATOM 784 CG LEU A 101 −18.909 23.905 12.286 1.00 9.07 C ATOM 785 CD1 LEU A 101 −17.675 23.904 13.156 1.00 13.36 C ATOM 786 CD2 LEU A 101 −19.878 22.797 12.691 1.00 12.74 C ATOM 787 N GLN A 102 −21.294 27.864 11.342 1.00 5.43 N ATOM 788 CA GLN A 102 −22.177 28.997 11.599 1.00 5.19 C ATOM 789 C GLN A 102 −23.543 28.772 10.970 1.00 6.32 C ATOM 790 O GLN A 102 −24.579 28.956 11.610 1.00 6.82 O ATOM 791 CB GLN A 102 −21.552 30.286 11.068 1.00 6.74 C ATOM 792 CG GLN A 102 −22.446 31.499 11.276 1.00 7.84 C ATOM 793 CD GLN A 102 −21.965 32.740 10.550 1.00 7.29 C ATOM 794 OE1 GLN A 102 −20.883 32.767 9.977 1.00 9.47 O ATOM 795 NE2 GLN A 102 −22.787 33.791 10.585 1.00 8.18 N ATOM 796 N HIS A 103 −23.552 28.370 9.699 1.00 5.94 N ATOM 797 CA HIS A 103 −24.801 28.171 9.002 1.00 6.08 C ATOM 798 C HIS A 103 −25.598 27.012 9.607 1.00 4.80 C ATOM 799 O HIS A 103 −26.801 27.111 9.797 1.00 6.26 O ATOM 800 CB HIS A 103 −24.531 27.925 7.515 1.00 6.90 C ATOM 801 CG HIS A 103 −25.677 28.278 6.631 1.00 7.96 C ATOM 802 ND1 HIS A 103 −25.565 28.282 5.256 1.00 8.59 N ATOM 803 CD2 HIS A 103 −26.945 28.655 6.910 1.00 6.64 C ATOM 804 CE1 HIS A 103 −26.719 28.655 4.728 1.00 8.29 C ATOM 805 NE2 HIS A 103 −27.581 28.872 5.708 1.00 9.02 N ATOM 806 N VAL A 104 −24.913 25.903 9.888 1.00 5.95 N ATOM 807 CA VAL A 104 −25.605 24.765 10.486 1.00 7.58 C ATOM 808 C VAL A 104 −26.224 25.153 11.843 1.00 5.80 C ATOM 809 O VAL A 104 −27.385 24.851 12.108 1.00 7.78 O ATOM 810 CB VAL A 104 −24.653 23.572 10.668 1.00 7.05 C ATOM 811 CG1 VAL A 104 −25.302 22.506 11.558 1.00 10.12 C ATOM 812 CG2 VAL A 104 −24.250 22.984 9.309 1.00 9.57 C ATOM 813 N ASP A 105 −25.434 25.831 12.676 1.00 6.23 N ATOM 814 CA ASP A 105 −25.933 26.244 13.994 1.00 6.14 C ATOM 815 C ASP A 105 −27.133 27.178 13.856 1.00 8.33 C ATOM 816 O ASP A 105 −28.112 27.052 14.592 1.00 8.56 O ATOM 817 CB ASP A 105 −24.839 26.905 14.843 1.00 7.42 C ATOM 818 CG ASP A 105 −23.776 25.920 15.336 1.00 13.92 C ATOM 819 OD1 ASP A 105 −24.061 24.704 15.406 1.00 16.13 O ATOM 820 OD2 ASP A 105 −22.648 26.361 15.663 1.00 13.33 O ATOM 821 N SER A 106 −27.082 28.111 12.903 1.00 7.27 N ATOM 822 CA ASER A 106 −28.184 29.047 12.712 0.33 8.06 C ATOM 823 C SER A 106 −29.453 28.338 12.241 1.00 9.29 C ATOM 824 O SER A 106 −30.557 28.661 12.670 1.00 12.36 O ATOM 825 CB ASER A 106 −27.791 30.152 11.727 0.33 12.36 C ATOM 826 OG ASER A 106 −28.878 31.033 11.504 0.33 11.64 O ATOM 827 CA BSER A 106 −28.189 29.044 12.739 0.33 7.72 C ATOM 828 CB BSER A 106 −27.798 30.224 11.836 0.33 8.33 C ATOM 829 OG BSER A 106 −27.502 29.800 10.519 0.33 9.09 O ATOM 830 CA CSER A 106 −28.187 29.046 12.697 0.33 8.20 C ATOM 831 CB CSER A 106 −27.805 30.112 11.671 0.33 14.56 C ATOM 832 OG CSER A 106 −26.705 30.866 12.126 0.33 10.99 O ATOM 833 N MET A 107 −29.301 27.365 11.344 1.00 7.49 N ATOM 834 CA AMET A 107 −30.442 26.604 10.845 0.50 10.61 C ATOM 835 C MET A 107 −31.031 25.708 11.936 1.00 6.77 C ATOM 836 O MET A 107 −32.255 25.615 12.087 1.00 11.21 O ATOM 837 CB AMET A 107 −30.024 25.765 9.629 0.50 11.62 C ATOM 838 CG AMET A 107 −31.142 24.962 8.981 0.50 11.62 C ATOM 839 SD AMET A 107 −32.524 25.957 8.382 0.50 17.80 S ATOM 840 CE AMET A 107 −31.659 27.299 7.589 0.50 16.49 C ATOM 841 CA BMET A 107 −30.454 26.617 10.859 0.50 6.28 C ATOM 842 CB BMET A 107 −30.076 25.798 9.625 0.50 11.75 C ATOM 843 CG BMET A 107 −29.649 26.659 8.460 0.50 12.02 C ATOM 844 SD BMET A 107 −30.974 27.746 7.914 0.50 26.78 S ATOM 845 CE BMET A 107 −32.093 26.557 7.189 0.50 15.11 C ATOM 846 N GLN A 108 −30.154 25.044 12.688 1.00 9.49 N ATOM 847 CA AGLN A 108 −30.611 24.118 13.720 0.50 9.57 C ATOM 848 C GLN A 108 −31.458 24.812 14.782 1.00 11.46 C ATOM 849 O GLN A 108 −32.441 24.243 15.262 1.00 12.43 O ATOM 850 CB AGLN A 108 −29.439 23.367 14.357 0.50 12.58 C ATOM 851 CG AGLN A 108 −28.938 22.209 13.504 0.50 12.65 C ATOM 852 CD AGLN A 108 −28.137 21.196 14.294 0.50 68.54 C ATOM 853 OE1 AGLN A 108 −28.661 20.161 14.699 0.50 23.41 O ATOM 854 NE2 AGLN A 108 −26.864 21.489 14.521 0.50 7.83 N ATOM 855 CA BGLN A 108 −30.589 24.119 13.737 0.50 8.69 C ATOM 856 CB BGLN A 108 −29.391 23.463 14.430 0.50 9.25 C ATOM 857 CG BGLN A 108 −29.780 22.432 15.483 0.50 13.14 C ATOM 858 CD BGLN A 108 −30.122 21.075 14.882 0.50 70.97 C ATOM 859 OE1 BGLN A 108 −29.236 20.263 14.616 0.50 17.19 O ATOM 860 NE2 BGLN A 108 −31.413 20.820 14.679 0.50 9.82 N ATOM 861 N LYS A 109 −31.099 26.046 15.133 1.00 10.35 N ATOM 862 CA LYS A 109 −31.860 26.757 16.166 1.00 12.18 C ATOM 863 C LYS A 109 −33.260 27.117 15.670 1.00 15.37 C ATOM 864 O LYS A 109 −34.181 27.259 16.477 1.00 15.02 O ATOM 865 CB LYS A 109 −31.119 28.010 16.647 1.00 12.62 C ATOM 866 CG LYS A 109 −31.207 29.149 15.643 1.00 24.20 C ATOM 867 CD LYS A 109 −30.473 30.401 16.074 1.00 26.44 C ATOM 868 CE LYS A 109 −30.940 31.602 15.256 1.00 17.15 C ATOM 869 NZ LYS A 109 −31.147 31.297 13.808 1.00 22.59 N ATOM 870 N ASP A 110 −33.420 27.265 14.352 1.00 11.64 N ATOM 871 CA ASP A 110 −34.731 27.502 13.748 1.00 14.09 C ATOM 872 C ASP A 110 −35.540 26.202 13.650 1.00 17.43 C ATOM 873 O ASP A 110 −36.768 26.227 13.596 1.00 16.72 O ATOM 874 CB ASP A 110 −34.603 28.125 12.349 1.00 16.62 C ATOM 875 CG ASP A 110 −33.858 29.459 12.349 1.00 35.51 C ATOM 876 OD1 ASP A 110 −33.892 30.183 13.363 1.00 27.26 O ATOM 877 OD2 ASP A 110 −33.242 29.795 11.314 1.00 33.71 O ATOM 878 N TYR A 111 −34.838 25.070 13.614 1.00 12.88 N ATOM 879 CA TYR A 111 −35.463 23.749 13.495 1.00 11.95 C ATOM 880 C TYR A 111 −34.929 22.816 14.570 1.00 14.36 C ATOM 881 O TYR A 111 −34.283 21.805 14.270 1.00 15.37 O ATOM 882 CB TYR A 111 −35.195 23.153 12.104 1.00 14.49 C ATOM 883 CG TYR A 111 −35.903 23.906 11.010 1.00 11.25 C ATOM 884 CD1 TYR A 111 −35.303 24.996 10.389 1.00 11.70 C ATOM 885 CD2 TYR A 111 −37.177 23.536 10.605 1.00 13.97 C ATOM 886 CE1 TYR A 111 −35.964 25.702 9.397 1.00 12.73 C ATOM 887 CE2 TYR A 111 −37.842 24.229 9.609 1.00 13.65 C ATOM 888 CZ TYR A 111 −37.234 25.306 9.013 1.00 13.00 C ATOM 889 OH TYR A 111 −37.903 25.994 8.027 1.00 17.94 O ATOM 890 N PRO A 112 −35.184 23.159 15.842 1.00 16.22 N ATOM 891 CA PRO A 112 −34.592 22.419 16.956 1.00 17.66 C ATOM 892 C PRO A 112 −35.069 20.974 16.951 1.00 18.24 C ATOM 893 O PRO A 112 −36.225 20.702 16.616 1.00 23.82 O ATOM 894 CB PRO A 112 −35.132 23.166 18.190 1.00 24.32 C ATOM 895 CG PRO A 112 −36.365 23.857 17.695 1.00 22.23 C ATOM 896 CD PRO A 112 −35.988 24.298 16.318 1.00 19.06 C ATOM 897 N GLY A 113 −34.176 20.058 17.295 1.00 21.11 N ATOM 898 CA GLY A 113 −34.537 18.657 17.369 1.00 27.87 C ATOM 899 C GLY A 113 −34.396 17.874 16.075 1.00 37.60 C ATOM 900 O GLY A 113 −34.388 16.645 16.105 1.00 26.73 O ATOM 901 N LEU A 114 −34.294 18.556 14.937 1.00 17.32 N ATOM 902 CA LEU A 114 −34.147 17.831 13.678 1.00 16.13 C ATOM 903 C LEU A 114 −32.712 17.349 13.481 1.00 14.38 C ATOM 904 O LEU A 114 −31.757 18.081 13.758 1.00 14.82 O ATOM 905 CB LEU A 114 −34.560 18.689 12.485 1.00 15.76 C ATOM 906 CG LEU A 114 −36.039 19.009 12.274 1.00 19.83 C ATOM 907 CD1 LEU A 114 −36.244 19.522 10.860 1.00 22.33 C ATOM 908 CD2 LEU A 114 −36.907 17.787 12.537 1.00 26.81 C ATOM 909 N PRO A 115 −32.559 16.110 12.993 1.00 14.51 N ATOM 910 CA PRO A 115 −31.241 15.578 12.631 1.00 14.94 C ATOM 911 C PRO A 115 −30.640 16.390 11.484 1.00 9.64 C ATOM 912 O PRO A 115 −31.386 16.881 10.636 1.00 12.08 O ATOM 913 CB PRO A 115 −31.554 14.159 12.140 1.00 16.54 C ATOM 914 CG PRO A 115 −32.911 13.846 12.664 1.00 25.57 C ATOM 915 CD PRO A 115 −33.640 15.148 12.735 1.00 14.61 C ATOM 916 N VAL A 116 −29.320 16.522 11.472 1.00 8.33 N ATOM 917 CA AVAL A 116 −28.656 17.245 10.396 0.50 6.55 C ATOM 918 C VAL A 116 −27.608 16.371 9.703 1.00 9.54 C ATOM 919 O VAL A 116 −26.774 15.730 10.337 1.00 9.56 O ATOM 920 CB AVAL A 116 −28.055 18.584 10.888 0.50 13.27 C ATOM 921 CG1 AVAL A 116 −27.021 18.342 11.977 0.50 10.54 C ATOM 922 CG2 AVAL A 116 −27.472 19.385 9.721 0.50 6.54 C ATOM 923 CA BVAL A 116 −28.606 17.265 10.430 0.50 11.46 C ATOM 924 CB BVAL A 116 −27.833 18.463 11.022 0.50 7.27 C ATOM 925 CG1 BVAL A 116 −26.972 19.144 9.954 0.50 10.48 C ATOM 926 CG2 BVAL A 116 −28.798 19.447 11.664 0.50 11.77 C ATOM 927 N PHE A 117 −27.694 16.350 8.377 1.00 8.25 N ATOM 928 CA PHE A 117 −26.766 15.613 7.523 1.00 6.73 C ATOM 929 C PHE A 117 −25.872 16.596 6.781 1.00 7.65 C ATOM 930 O PHE A 117 −26.221 17.782 6.646 1.00 7.95 O ATOM 931 CB PHE A 117 −27.544 14.791 6.495 1.00 7.19 C ATOM 932 CG PHE A 117 −28.342 13.659 7.089 1.00 9.66 C ATOM 933 CD1 PHE A 117 −29.578 13.888 7.675 1.00 9.86 C ATOM 934 CD2 PHE A 117 −27.858 12.366 7.035 1.00 11.39 C ATOM 935 CE1 PHE A 117 −30.315 12.846 8.221 1.00 11.17 C ATOM 936 CE2 PHE A 117 −28.592 11.316 7.576 1.00 12.02 C ATOM 937 CZ PHE A 117 −29.810 11.552 8.167 1.00 12.26 C ATOM 938 N LEU A 118 −24.751 16.093 6.272 1.00 6.39 N ATOM 939 CA LEU A 118 −23.844 16.851 5.409 1.00 6.79 C ATOM 940 C LEU A 118 −23.696 16.104 4.084 1.00 9.58 C ATOM 941 O LEU A 118 −23.659 14.869 4.053 1.00 10.15 O ATOM 942 CB LEU A 118 −22.467 16.990 6.054 1.00 8.39 C ATOM 943 CG LEU A 118 −22.423 17.678 7.421 1.00 7.65 C ATOM 944 CD1 LEU A 118 −21.069 17.514 8.065 1.00 12.05 C ATOM 945 CD2 LEU A 118 −22.805 19.163 7.274 1.00 14.26 C ATOM 946 N LEU A 119 −23.606 16.848 2.989 1.00 6.75 N ATOM 947 CA LEU A 119 −23.262 16.262 1.695 1.00 6.84 C ATOM 948 C LEU A 119 −22.159 17.111 1.091 1.00 6.93 C ATOM 949 O LEU A 119 −22.288 18.341 1.039 1.00 9.68 O ATOM 950 CB LEU A 119 −24.478 16.235 0.780 1.00 9.51 C ATOM 951 CG LEU A 119 −24.279 15.572 −0.595 1.00 8.88 C ATOM 952 CD1 LEU A 119 −25.576 14.929 −1.069 1.00 14.75 C ATOM 953 CD2 LEU A 119 −23.738 16.566 −1.628 1.00 12.64 C ATOM 954 N GLY A 120 −21.076 16.486 0.640 1.00 5.97 N ATOM 955 CA GLY A 120 −19.986 17.265 0.088 1.00 6.20 C ATOM 956 C GLY A 120 −19.321 16.567 −1.078 1.00 7.47 C ATOM 957 O GLY A 120 −19.260 15.334 −1.112 1.00 8.48 O ATOM 958 N HIS A 121 −18.805 17.354 −2.013 1.00 4.99 N ATOM 959 CA HIS A 121 −18.051 16.840 −3.158 1.00 5.24 C ATOM 960 C HIS A 121 −16.656 17.442 −3.172 1.00 4.93 C ATOM 961 O HIS A 121 −16.494 18.663 −3.004 1.00 6.29 O ATOM 962 CB HIS A 121 −18.791 17.217 −4.456 1.00 6.08 C ATOM 963 CG HIS A 121 −17.985 17.032 −5.712 1.00 7.22 C ATOM 964 ND1 HIS A 121 −17.405 15.831 −6.075 1.00 8.06 N ATOM 965 CD2 HIS A 121 −17.688 17.906 −6.707 1.00 6.53 C ATOM 966 CE1 HIS A 121 −16.785 15.977 −7.238 1.00 8.61 C ATOM 967 NE2 HIS A 121 −16.941 17.227 −7.641 1.00 7.27 N ATOM 968 N SER A 122 −15.635 16.614 −3.358 1.00 5.44 N ATOM 969 CA SER A 122 −14.288 17.105 −3.623 1.00 6.10 C ATOM 970 C SER A 122 −13.779 17.939 −2.431 1.00 7.18 C ATOM 971 O SER A 122 −13.808 17.447 −1.292 1.00 6.60 O ATOM 972 CB SER A 122 −14.240 17.852 −4.976 1.00 7.68 C ATOM 973 OG SER A 122 −12.925 17.935 −5.480 1.00 8.60 O ATOM 974 N MET A 123 −13.298 19.163 −2.648 1.00 7.05 N ATOM 975 CA MET A 123 −12.930 20.012 −1.510 1.00 6.85 C ATOM 976 C MET A 123 −14.067 20.114 −0.498 1.00 5.95 C ATOM 977 O MET A 123 −13.825 20.180 0.715 1.00 6.61 O ATOM 978 CB MET A 123 −12.544 21.418 −1.969 1.00 6.44 C ATOM 979 CG MET A 123 −12.132 22.321 −0.808 1.00 6.74 C ATOM 980 SD MET A 123 −11.872 24.035 −1.346 1.00 9.51 S ATOM 981 CE MET A 123 −13.527 24.679 −1.392 1.00 11.77 C ATOM 982 N GLY A 124 −15.294 20.162 −0.991 1.00 5.76 N ATOM 983 CA GLY A 124 −16.465 20.242 −0.134 1.00 5.33 C ATOM 984 C GLY A 124 −16.644 19.005 0.733 1.00 6.28 C ATOM 985 O GLY A 124 −17.250 19.080 1.807 1.00 7.72 O ATOM 986 N GLY A 125 −16.131 17.871 0.258 1.00 6.88 N ATOM 987 CA GLY A 125 −16.123 16.647 1.048 1.00 6.32 C ATOM 988 C GLY A 125 −15.096 16.702 2.164 1.00 7.06 C ATOM 989 O GLY A 125 −15.362 16.219 3.275 1.00 8.26 O ATOM 990 N ALA A 126 −13.936 17.291 1.906 1.00 6.65 N ATOM 991 CA ALA A 126 −12.967 17.542 2.966 1.00 7.07 C ATOM 992 C ALA A 126 −13.560 18.468 4.027 1.00 8.51 C ATOM 993 O ALA A 126 −13.390 18.234 5.232 1.00 8.99 O ATOM 994 CB ALA A 126 −11.685 18.140 2.394 1.00 9.00 C ATOM 995 N ILE A 127 −14.256 19.510 3.587 1.00 5.80 N ATOM 996 CA ILE A 127 −14.899 20.425 4.512 1.00 5.81 C ATOM 997 C ILE A 127 −15.919 19.663 5.359 1.00 7.22 C ATOM 998 O ILE A 127 −15.978 19.846 6.586 1.00 8.40 O ATOM 999 CB ILE A 127 −15.560 21.585 3.757 1.00 5.20 C ATOM 1000 CG1 ILE A 127 −14.479 22.471 3.125 1.00 6.80 C ATOM 1001 CG2 ILE A 127 −16.455 22.395 4.692 1.00 7.18 C ATOM 1002 CD1 ILE A 127 −14.991 23.467 2.072 1.00 8.65 C ATOM 1003 N ALA A 128 −16.708 18.794 4.735 1.00 6.54 N ATOM 1004 CA ALA A 128 −17.685 17.983 5.472 1.00 6.61 C ATOM 1005 C ALA A 128 −17.014 17.098 6.525 1.00 6.98 C ATOM 1006 O ALA A 128 −17.470 17.038 7.676 1.00 8.44 O ATOM 1007 CB ALA A 128 −18.527 17.138 4.522 1.00 8.15 C ATOM 1008 N ILE A 129 −15.951 16.402 6.138 1.00 6.43 N ATOM 1009 CA ILE A 129 −15.234 15.541 7.073 1.00 8.20 C ATOM 1010 C ILE A 129 −14.742 16.355 8.274 1.00 7.24 C ATOM 1011 O ILE A 129 −14.921 15.943 9.432 1.00 9.40 O ATOM 1012 CB ILE A 129 −14.056 14.835 6.372 1.00 7.21 C ATOM 1013 CG1 ILE A 129 −14.577 13.788 5.374 1.00 8.59 C ATOM 1014 CG2 ILE A 129 −13.099 14.196 7.392 1.00 8.65 C ATOM 1015 CD1 ILE A 129 −13.518 13.302 4.381 1.00 8.43 C ATOM 1016 N LEU A 130 −14.109 17.494 8.016 1.00 7.88 N ATOM 1017 CA LEU A 130 −13.564 18.322 9.090 1.00 7.26 C ATOM 1018 C LEU A 130 −14.648 18.930 9.968 1.00 8.38 C ATOM 1019 O LEU A 130 −14.440 19.099 11.175 1.00 11.78 O ATOM 1020 CB LEU A 130 −12.629 19.396 8.522 1.00 7.43 C ATOM 1021 CG LEU A 130 −11.379 18.824 7.851 1.00 7.20 C ATOM 1022 CD1 LEU A 130 −10.588 19.932 7.164 1.00 11.26 C ATOM 1023 CD2 LEU A 130 −10.499 18.088 8.856 1.00 11.11 C ATOM 1024 N THR A 131 −15.792 19.247 9.381 1.00 6.76 N ATOM 1025 CA THR A 131 −16.937 19.765 10.120 1.00 7.15 C ATOM 1026 C THR A 131 −17.469 18.709 11.090 1.00 10.49 C ATOM 1027 O THR A 131 −17.694 18.990 12.278 1.00 10.09 O ATOM 1028 CB THR A 131 −18.044 20.221 9.142 1.00 6.73 C ATOM 1029 OG1 THR A 131 −17.544 21.303 8.342 1.00 9.73 O ATOM 1030 CG2 THR A 131 −19.293 20.695 9.876 1.00 9.04 C ATOM 1031 N ALA A 132 −17.667 17.493 10.591 1.00 8.54 N ATOM 1032 CA ALA A 132 −18.145 16.401 11.429 1.00 10.74 C ATOM 1033 C ALA A 132 −17.152 16.098 12.545 1.00 13.98 C ATOM 1034 O ALA A 132 −17.559 15.799 13.674 1.00 17.35 O ATOM 1035 CB ALA A 132 −18.395 15.153 10.588 1.00 12.21 C ATOM 1036 N ALA A 133 −15.862 16.190 12.247 1.00 11.80 N ATOM 1037 CA ALA A 133 −14.836 15.861 13.228 1.00 13.45 C ATOM 1038 C ALA A 133 −14.746 16.916 14.325 1.00 17.15 C ATOM 1039 O ALA A 133 −14.327 16.619 15.451 1.00 19.66 O ATOM 1040 CB ALA A 133 −13.475 15.669 12.546 1.00 15.60 C ATOM 1041 N GLU A 134 −15.139 18.143 14.001 1.00 16.89 N ATOM 1042 CA GLU A 134 −15.107 19.240 14.961 1.00 17.80 C ATOM 1043 C GLU A 134 −16.272 19.188 15.952 1.00 21.56 C ATOM 1044 O GLU A 134 −16.207 19.805 17.023 1.00 21.34 O ATOM 1045 CB GLU A 134 −15.086 20.585 14.232 1.00 19.70 C ATOM 1046 CG GLU A 134 −15.042 21.779 15.166 1.00 31.66 C ATOM 1047 CD GLU A 134 −14.422 22.997 14.524 1.00 77.78 C ATOM 1048 OE1 GLU A 134 −13.675 22.834 13.534 1.00 29.11 O ATOM 1049 OE2 GLU A 134 −14.678 24.116 15.017 1.00 32.70 O ATOM 1050 N ARG A 135 −17.328 18.457 15.597 1.00 15.43 N ATOM 1051 CA ARG A 135 −18.489 18.264 16.470 1.00 14.20 C ATOM 1052 C ARG A 135 −18.795 16.777 16.633 1.00 15.41 C ATOM 1053 O ARG A 135 −19.804 16.274 16.129 1.00 16.46 O ATOM 1054 CB ARG A 135 −19.717 18.994 15.924 1.00 15.89 C ATOM 1055 CG ARG A 135 −19.520 20.485 15.716 1.00 19.46 C ATOM 1056 CD ARG A 135 −19.647 21.282 17.015 1.00 22.44 C ATOM 1057 NE ARG A 135 −19.498 22.713 16.762 1.00 17.05 N ATOM 1058 CZ ARG A 135 −20.503 23.518 16.428 1.00 13.79 C ATOM 1059 NH1 ARG A 135 −21.738 23.043 16.315 1.00 15.86 N ATOM 1060 NH2 ARG A 135 −20.264 24.802 16.195 1.00 15.95 N ATOM 1061 N PRO A 136 −17.921 16.062 17.353 1.00 20.51 N ATOM 1062 CA PRO A 136 −18.056 14.607 17.494 1.00 24.54 C ATOM 1063 C PRO A 136 −19.441 14.177 17.975 1.00 29.40 C ATOM 1064 O PRO A 136 −19.924 14.677 18.994 1.00 23.65 O ATOM 1065 CB PRO A 136 −17.007 14.262 18.554 1.00 27.33 C ATOM 1066 CG PRO A 136 −16.000 15.361 18.471 1.00 33.77 C ATOM 1067 CD PRO A 136 −16.774 16.596 18.109 1.00 22.45 C ATOM 1068 N GLY A 137 −20.063 13.257 17.244 1.00 19.62 N ATOM 1069 CA GLY A 137 −21.346 12.689 17.613 1.00 16.56 C ATOM 1070 C GLY A 137 −22.563 13.519 17.260 1.00 18.57 C ATOM 1071 O GLY A 137 −23.687 13.134 17.559 1.00 24.49 O ATOM 1072 N HIS A 138 −22.347 14.657 16.605 1.00 14.73 N ATOM 1073 CA HIS A 138 −23.423 15.610 16.384 1.00 14.81 C ATOM 1074 C HIS A 138 −24.243 15.369 15.103 1.00 13.75 C ATOM 1075 O HIS A 138 −25.472 15.419 15.122 1.00 17.01 O ATOM 1076 CB HIS A 138 −22.853 17.027 16.385 1.00 17.64 C ATOM 1077 CG HIS A 138 −23.888 18.087 16.192 1.00 19.02 C ATOM 1078 ND1 HIS A 138 −24.835 18.385 17.150 1.00 24.37 N ATOM 1079 CD2 HIS A 138 −24.131 18.918 15.151 1.00 21.19 C ATOM 1080 CE1 HIS A 138 −25.615 19.354 16.706 1.00 53.43 C ATOM 1081 NE2 HIS A 138 −25.210 19.695 15.496 1.00 28.81 N ATOM 1082 N PHE A 139 −23.557 15.105 13.993 1.00 12.98 N ATOM 1083 CA PHE A 139 −24.235 14.934 12.708 1.00 12.74 C ATOM 1084 C PHE A 139 −24.824 13.537 12.536 1.00 8.88 C ATOM 1085 O PHE A 139 −24.244 12.555 13.007 1.00 12.86 O ATOM 1086 CB PHE A 139 −23.280 15.293 11.558 1.00 11.40 C ATOM 1087 CG PHE A 139 −22.933 16.751 11.522 1.00 8.97 C ATOM 1088 CD1 PHE A 139 −23.765 17.647 10.875 1.00 10.65 C ATOM 1089 CD2 PHE A 139 −21.807 17.228 12.169 1.00 10.08 C ATOM 1090 CE1 PHE A 139 −23.456 19.002 10.856 1.00 11.55 C ATOM 1091 CE2 PHE A 139 −21.501 18.580 12.162 1.00 9.46 C ATOM 1092 CZ PHE A 139 −22.330 19.464 11.501 1.00 11.90 C ATOM 1093 N ALA A 140 −25.969 13.462 11.872 1.00 10.10 N ATOM 1094 CA ALA A 140 −26.681 12.201 11.680 1.00 11.80 C ATOM 1095 C ALA A 140 −26.034 11.356 10.589 1.00 12.36 C ATOM 1096 O ALA A 140 −26.193 10.135 10.557 1.00 13.34 O ATOM 1097 CB ALA A 140 −28.128 12.459 11.333 1.00 12.22 C ATOM 1098 N GLY A 141 −25.327 12.009 9.675 1.00 9.31 N ATOM 1099 CA GLY A 141 −24.774 11.289 8.546 1.00 9.56 C ATOM 1100 C GLY A 141 −24.130 12.212 7.548 1.00 11.98 C ATOM 1101 O GLY A 141 −24.391 13.420 7.525 1.00 10.18 O ATOM 1102 N MET A 142 −23.292 11.614 6.711 1.00 8.32 N ATOM 1103 CA AMET A 142 −22.502 12.331 5.725 0.70 8.58 C ATOM 1104 C MET A 142 −22.554 11.573 4.389 1.00 9.98 C ATOM 1105 O MET A 142 −22.320 10.356 4.367 1.00 10.51 O ATOM 1106 CB AMET A 142 −21.067 12.360 6.237 0.70 25.98 C ATOM 1107 CG AMET A 142 −20.126 13.326 5.579 0.70 16.80 C ATOM 1108 SD AMET A 142 −18.699 13.543 6.679 0.70 15.44 S ATOM 1109 CE AMET A 142 −18.032 11.891 6.773 0.70 13.72 C ATOM 1110 CA BMET A 142 −22.589 12.353 5.680 0.30 8.38 C ATOM 1111 CB BMET A 142 −21.163 12.652 6.104 0.30 4.61 C ATOM 1112 CG BMET A 142 −21.010 13.930 6.885 0.30 26.62 C ATOM 1113 SD BMET A 142 −19.322 14.124 7.459 0.30 21.03 S ATOM 1114 CE BMET A 142 −18.407 13.324 6.145 0.30 22.67 C ATOM 1115 N VAL A 143 −22.825 12.281 3.299 1.00 7.01 N ATOM 1116 CA VAL A 143 −22.730 11.708 1.964 1.00 7.21 C ATOM 1117 C VAL A 143 −21.561 12.389 1.268 1.00 7.22 C ATOM 1118 O VAL A 143 −21.534 13.624 1.135 1.00 7.86 O ATOM 1119 CB VAL A 143 −24.017 11.957 1.159 1.00 8.34 C ATOM 1120 CG1 VAL A 143 −23.839 11.460 −0.286 1.00 10.34 C ATOM 1121 CG2 VAL A 143 −25.207 11.275 1.833 1.00 10.57 C ATOM 1122 N LEU A 144 −20.576 11.601 0.853 1.00 5.85 N ATOM 1123 CA LEU A 144 −19.357 12.139 0.276 1.00 6.51 C ATOM 1124 C LEU A 144 −19.222 11.661 −1.160 1.00 8.86 C ATOM 1125 O LEU A 144 −19.195 10.456 −1.439 1.00 7.94 O ATOM 1126 CB LEU A 144 −18.143 11.680 1.084 1.00 6.27 C ATOM 1127 CG LEU A 144 −18.117 12.083 2.559 1.00 9.97 C ATOM 1128 CD1 LEU A 144 −16.959 11.359 3.232 1.00 11.52 C ATOM 1129 CD2 LEU A 144 −17.983 13.615 2.693 1.00 11.05 C ATOM 1130 N ILE A 145 −19.179 12.618 −2.079 1.00 5.85 N ATOM 1131 CA ILE A 145 −18.973 12.315 −3.490 1.00 6.29 C ATOM 1132 C ILE A 145 −17.545 12.689 −3.844 1.00 6.81 C ATOM 1133 O ILE A 145 −17.194 13.876 −3.904 1.00 6.91 O ATOM 1134 CB ILE A 145 −19.957 13.103 −4.377 1.00 5.41 C ATOM 1135 CG1 ILE A 145 −21.400 12.836 −3.954 1.00 9.22 C ATOM 1136 CG2 ILE A 145 −19.742 12.726 −5.846 1.00 8.27 C ATOM 1137 CD1 ILE A 145 −22.431 13.717 −4.651 1.00 9.95 C ATOM 1138 N SER A 146 −16.689 11.689 −4.034 1.00 6.84 N ATOM 1139 CA SER A 146 −15.301 11.934 −4.411 1.00 6.91 C ATOM 1140 C SER A 146 −14.655 12.966 −3.493 1.00 7.51 C ATOM 1141 O SER A 146 −14.114 13.975 −3.958 1.00 7.48 O ATOM 1142 CB SER A 146 −15.201 12.439 −5.857 1.00 8.55 C ATOM 1143 OG SER A 146 −16.035 11.684 −6.705 1.00 19.57 O ATOM 1144 N PRO A 147 −14.668 12.714 −2.178 1.00 7.19 N ATOM 1145 CA PRO A 147 −14.114 13.708 −1.250 1.00 6.02 C ATOM 1146 C PRO A 147 −12.612 13.828 −1.423 1.00 8.82 C ATOM 1147 O PRO A 147 −11.933 12.854 −1.765 1.00 8.83 O ATOM 1148 CB PRO A 147 −14.431 13.108 0.123 1.00 7.28 C ATOM 1149 CG PRO A 147 −14.419 11.598 −0.149 1.00 7.97 C ATOM 1150 CD PRO A 147 −15.119 11.491 −1.486 1.00 7.21 C ATOM 1151 N LEU A 148 −12.077 15.017 −1.183 1.00 7.64 N ATOM 1152 CA LEU A 148 −10.643 15.212 −1.171 1.00 7.57 C ATOM 1153 C LEU A 148 −10.037 14.612 0.100 1.00 10.69 C ATOM 1154 O LEU A 148 −10.082 15.230 1.180 1.00 13.01 O ATOM 1155 CB LEU A 148 −10.308 16.702 −1.295 1.00 10.01 C ATOM 1156 CG LEU A 148 −8.831 17.084 −1.238 1.00 13.54 C ATOM 1157 CD1 LEU A 148 −8.050 16.349 −2.318 1.00 18.01 C ATOM 1158 CD2 LEU A 148 −8.660 18.592 −1.378 1.00 19.64 C ATOM 1159 N VAL A 149 −9.491 13.403 −0.029 1.00 10.28 N ATOM 1160 CA VAL A 149 −8.837 12.724 1.087 1.00 9.11 C ATOM 1161 C VAL A 149 −7.359 12.529 0.775 1.00 11.36 C ATOM 1162 O VAL A 149 −6.496 12.909 1.560 1.00 13.79 O ATOM 1163 CB VAL A 149 −9.514 11.374 1.410 1.00 7.75 C ATOM 1164 CG1 VAL A 149 −8.733 10.636 2.512 1.00 9.82 C ATOM 1165 CG2 VAL A 149 −10.957 11.592 1.816 1.00 8.89 C ATOM 1166 N LEU A 150 −7.069 11.934 −0.380 1.00 10.74 N ATOM 1167 CA LEU A 150 −5.705 11.867 −0.886 1.00 12.38 C ATOM 1168 C LEU A 150 −5.711 12.416 −2.295 1.00 13.20 C ATOM 1169 O LEU A 150 −6.533 12.017 −3.119 1.00 14.22 O ATOM 1170 CB LEU A 150 −5.185 10.428 −0.916 1.00 13.51 C ATOM 1171 CG LEU A 150 −4.880 9.789 0.439 1.00 17.14 C ATOM 1172 CD1 LEU A 150 −3.807 10.577 1.181 1.00 19.78 C ATOM 1173 CD2 LEU A 150 −4.453 8.333 0.248 1.00 21.23 C ATOM 1174 N ALA A 151 −4.803 13.338 −2.572 1.00 12.30 N ATOM 1175 CA ALA A 151 −4.701 13.879 −3.917 1.00 16.69 C ATOM 1176 C ALA A 151 −3.972 12.890 −4.819 1.00 15.92 C ATOM 1177 O ALA A 151 −3.240 12.021 −4.344 1.00 15.20 O ATOM 1178 CB ALA A 151 −3.981 15.220 −3.893 1.00 20.19 C ATOM 1179 N ASN A 152 −4.191 13.011 −6.120 1.00 14.44 N ATOM 1180 CA ASN A 152 −3.363 12.292 −7.071 1.00 13.52 C ATOM 1181 C ASN A 152 −1.896 12.543 −6.728 1.00 14.72 C ATOM 1182 O ASN A 152 −1.469 13.694 −6.634 1.00 15.93 O ATOM 1183 CB ASN A 152 −3.674 12.764 −8.487 1.00 19.76 C ATOM 1184 CG ASN A 152 −2.809 12.089 −9.524 1.00 18.69 C ATOM 1185 OD1 ASN A 152 −1.632 12.417 −9.674 1.00 20.74 O ATOM 1186 ND2 ASN A 152 −3.389 11.138 −10.251 1.00 23.13 N ATOM 1187 N PRO A 153 −1.122 11.467 −6.513 1.00 16.79 N ATOM 1188 CA PRO A 153 0.264 11.579 −6.041 1.00 17.04 C ATOM 1189 C PRO A 153 1.151 12.434 −6.946 1.00 16.59 C ATOM 1190 O PRO A 153 1.901 13.272 −6.445 1.00 17.20 O ATOM 1191 CB PRO A 153 0.749 10.125 −6.034 1.00 23.14 C ATOM 1192 CG PRO A 153 −0.491 9.322 −5.850 1.00 26.11 C ATOM 1193 CD PRO A 153 −1.570 10.065 −6.589 1.00 18.51 C ATOM 1194 N GLU A 154 1.072 12.222 −8.254 1.00 17.01 N ATOM 1195 CA GLU A 154 1.860 13.019 −9.191 1.00 17.94 C ATOM 1196 C GLU A 154 1.463 14.494 −9.151 1.00 16.34 C ATOM 1197 O GLU A 154 2.329 15.369 −9.141 1.00 16.77 O ATOM 1198 CB GLU A 154 1.754 12.464 −10.616 1.00 19.72 C ATOM 1199 CG GLU A 154 2.514 11.160 −10.810 1.00 56.06 C ATOM 1200 CD GLU A 154 2.713 10.806 −12.270 1.00 91.32 C ATOM 1201 OE1 GLU A 154 2.125 11.488 −13.136 1.00 55.91 O ATOM 1202 OE2 GLU A 154 3.462 9.845 −12.549 1.00 63.05 O ATOM 1203 N SER A 155 0.161 14.767 −9.124 1.00 14.06 N ATOM 1204 CA SER A 155 −0.333 16.141 −9.044 1.00 13.04 C ATOM 1205 C SER A 155 0.097 16.835 −7.752 1.00 13.20 C ATOM 1206 O SER A 155 0.483 18.007 −7.764 1.00 15.06 O ATOM 1207 CB SER A 155 −1.856 16.180 −9.150 1.00 19.70 C ATOM 1208 OG SER A 155 −2.293 15.617 −10.374 1.00 24.81 O ATOM 1209 N ALA A 156 0.018 16.113 −6.641 1.00 13.13 N ATOM 1210 CA ALA A 156 0.429 16.669 −5.357 1.00 14.25 C ATOM 1211 C ALA A 156 1.913 17.014 −5.368 1.00 14.95 C ATOM 1212 O ALA A 156 2.321 18.091 −4.916 1.00 13.46 O ATOM 1213 CB ALA A 156 0.118 15.696 −4.224 1.00 16.70 C ATOM 1214 N THR A 157 2.723 16.098 −5.890 1.00 13.19 N ATOM 1215 CA THR A 157 4.164 16.321 −5.953 1.00 12.51 C ATOM 1216 C THR A 157 4.494 17.494 −6.868 1.00 11.38 C ATOM 1217 O THR A 157 5.311 18.351 −6.521 1.00 13.00 O ATOM 1218 CB THR A 157 4.897 15.066 −6.435 1.00 16.00 C ATOM 1219 OG1 THR A 157 4.623 13.991 −5.527 1.00 20.31 O ATOM 1220 CG2 THR A 157 6.400 15.307 −6.485 1.00 16.90 C ATOM 1221 N THR A 158 3.858 17.525 −8.036 1.00 11.66 N ATOM 1222 CA THR A 158 4.036 18.639 −8.965 1.00 12.58 C ATOM 1223 C THR A 158 3.720 19.944 −8.250 1.00 12.22 C ATOM 1224 O THR A 158 4.459 20.927 −8.360 1.00 11.34 O ATOM 1225 CB THR A 158 3.119 18.502 −10.194 1.00 13.07 C ATOM 1226 OG1 THR A 158 3.539 17.373 −10.972 1.00 16.60 O ATOM 1227 CG2 THR A 158 3.174 19.755 −11.065 1.00 12.95 C ATOM 1228 N PHE A 159 2.620 19.962 −7.506 1.00 10.44 N ATOM 1229 CA PHE A 159 2.245 21.202 −6.850 1.00 11.72 C ATOM 1230 C PHE A 159 3.243 21.604 −5.765 1.00 9.72 C ATOM 1231 O PHE A 159 3.589 22.777 −5.652 1.00 11.95 O ATOM 1232 CB PHE A 159 0.842 21.161 −6.256 1.00 10.51 C ATOM 1233 CG PHE A 159 0.509 22.417 −5.524 1.00 12.93 C ATOM 1234 CD1 PHE A 159 0.146 23.552 −6.224 1.00 12.61 C ATOM 1235 CD2 PHE A 159 0.658 22.492 −4.150 1.00 13.42 C ATOM 1236 CE1 PHE A 159 −0.113 24.742 −5.566 1.00 15.13 C ATOM 1237 CE2 PHE A 159 0.399 23.682 −3.479 1.00 12.40 C ATOM 1238 CZ PHE A 159 0.013 24.805 −4.189 1.00 11.69 C ATOM 1239 N LYS A 160 3.699 20.645 −4.969 1.00 11.04 N ATOM 1240 CA LYS A 160 4.644 20.969 −3.906 1.00 13.94 C ATOM 1241 C LYS A 160 5.937 21.531 −4.483 1.00 14.48 C ATOM 1242 O LYS A 160 6.520 22.463 −3.936 1.00 14.62 O ATOM 1243 CB LYS A 160 4.933 19.743 −3.041 1.00 14.06 C ATOM 1244 CG LYS A 160 3.750 19.302 −2.200 1.00 16.18 C ATOM 1245 CD LYS A 160 4.049 18.014 −1.454 1.00 19.05 C ATOM 1246 CE LYS A 160 2.930 17.694 −0.473 1.00 30.54 C ATOM 1247 NZ LYS A 160 3.310 16.609 0.472 1.00 58.66 N ATOM 1248 N VAL A 161 6.391 20.961 −5.591 1.00 13.06 N ATOM 1249 CA VAL A 161 7.601 21.457 −6.237 1.00 17.55 C ATOM 1250 C VAL A 161 7.391 22.878 −6.766 1.00 15.74 C ATOM 1251 O VAL A 161 8.248 23.749 −6.605 1.00 14.78 O ATOM 1252 CB VAL A 161 8.044 20.524 −7.372 1.00 14.83 C ATOM 1253 CG1 VAL A 161 9.160 21.173 −8.186 1.00 19.24 C ATOM 1254 CG2 VAL A 161 8.494 19.183 −6.797 1.00 18.97 C ATOM 1255 N LEU A 162 6.239 23.110 −7.380 1.00 11.62 N ATOM 1256 CA LEU A 162 5.875 24.434 −7.867 1.00 10.78 C ATOM 1257 C LEU A 162 5.815 25.443 −6.726 1.00 15.67 C ATOM 1258 O LEU A 162 6.360 26.543 −6.826 1.00 14.46 O ATOM 1259 CB LEU A 162 4.520 24.381 −8.572 1.00 14.81 C ATOM 1260 CG LEU A 162 3.973 25.727 −9.046 1.00 22.23 C ATOM 1261 CD1 LEU A 162 4.800 26.249 −10.206 1.00 23.30 C ATOM 1262 CD2 LEU A 162 2.507 25.604 −9.439 1.00 24.52 C ATOM 1263 N ALA A 163 5.148 25.070 −5.639 1.00 11.29 N ATOM 1264 CA ALA A 163 4.999 25.983 −4.509 1.00 14.76 C ATOM 1265 C ALA A 163 6.362 26.338 −3.922 1.00 14.91 C ATOM 1266 O ALA A 163 6.602 27.491 −3.560 1.00 16.78 O ATOM 1267 CB ALA A 163 4.086 25.382 −3.442 1.00 14.03 C ATOM 1268 N ALA A 164 7.250 25.351 −3.835 1.00 13.62 N ATOM 1269 CA ALA A 164 8.598 25.582 −3.322 1.00 18.16 C ATOM 1270 C ALA A 164 9.400 26.525 −4.226 1.00 23.79 C ATOM 1271 O ALA A 164 10.109 27.402 −3.732 1.00 18.76 O ATOM 1272 CB ALA A 164 9.331 24.262 −3.137 1.00 20.61 C ATOM 1273 N LYS A 165 9.297 26.339 −5.544 1.00 17.69 N ATOM 1274 CA LYS A 165 9.950 27.243 −6.494 1.00 23.27 C ATOM 1275 C LYS A 165 9.456 28.657 −6.279 1.00 23.11 C ATOM 1276 O LYS A 165 10.238 29.600 −6.157 1.00 33.57 O ATOM 1277 CB LYS A 165 9.604 26.885 −7.940 1.00 30.74 C ATOM 1278 CG LYS A 165 10.148 25.590 −8.486 1.00 58.56 C ATOM 1279 CD LYS A 165 10.057 25.660 −10.004 1.00 28.67 C ATOM 1280 CE LYS A 165 9.648 24.348 −10.632 1.00 63.54 C ATOM 1281 NZ LYS A 165 9.245 24.586 −12.048 1.00 25.56 N ATOM 1282 N VAL A 166 8.137 28.800 −6.273 1.00 19.68 N ATOM 1283 CA VAL A 166 7.504 30.102 −6.156 1.00 19.36 C ATOM 1284 C VAL A 166 7.910 30.804 −4.862 1.00 38.58 C ATOM 1285 O VAL A 166 8.095 32.019 −4.840 1.00 41.10 O ATOM 1286 CB VAL A 166 5.966 29.992 −6.274 1.00 23.38 C ATOM 1287 CG1 VAL A 166 5.300 31.297 −5.869 1.00 33.39 C ATOM 1288 CG2 VAL A 166 5.576 29.597 −7.698 1.00 19.99 C ATOM 1289 N LEU A 167 8.069 30.031 −3.793 1.00 30.39 N ATOM 1290 CA LEU A 167 8.493 30.578 −2.504 1.00 29.35 C ATOM 1291 C LEU A 167 10.005 30.798 −2.400 1.00 37.42 C ATOM 1292 O LEU A 167 10.451 31.869 −1.989 1.00 45.82 O ATOM 1293 CB LEU A 167 8.033 29.670 −1.359 1.00 36.36 C ATOM 1294 CG LEU A 167 8.823 29.820 −0.053 1.00 72.40 C ATOM 1295 CD1 LEU A 167 8.542 31.166 0.601 1.00 72.35 C ATOM 1296 CD2 LEU A 167 8.525 28.677 0.910 1.00 57.03 C ATOM 1297 N ASN A 168 10.787 29.784 −2.765 1.00 27.55 N ATOM 1298 CA ASN A 168 12.237 29.810 −2.569 1.00 27.38 C ATOM 1299 C ASN A 168 13.020 30.567 −3.639 1.00 50.32 C ATOM 1300 O ASN A 168 14.246 30.674 −3.565 1.00 38.60 O ATOM 1301 CB ASN A 168 12.791 28.387 −2.456 1.00 31.18 C ATOM 1302 CG ASN A 168 12.355 27.689 −1.185 1.00 60.71 C ATOM 1303 OD1 ASN A 168 12.552 26.483 −1.028 1.00 56.08 O ATOM 1304 ND2 ASN A 168 11.759 28.443 −0.268 1.00 64.87 N ATOM 1305 N SER A 169 12.313 31.077 −4.639 1.00 23.88 N ATOM 1306 CA SER A 169 12.939 31.844 −5.708 1.00 29.73 C ATOM 1307 C SER A 169 12.086 33.057 −6.050 1.00 22.64 C ATOM 1308 CB SER A 169 13.123 30.976 −6.957 1.00 35.25 C ATOM 1309 OG SER A 169 13.964 29.866 −6.694 1.00 55.90 O ATOM 1310 O SER A 169 12.359 33.753 −7.029 1.00 27.12 O ATOM 1311 N VAL A 170 11.059 33.298 −5.237 1.00 20.95 N ATOM 1312 CA VAL A 170 10.077 34.351 −5.489 1.00 17.05 C ATOM 1313 C VAL A 170 9.765 34.510 −6.985 1.00 23.05 C ATOM 1314 O VAL A 170 9.865 35.603 −7.545 1.00 22.27 O ATOM 1315 CB VAL A 170 10.503 35.708 −4.858 1.00 23.73 C ATOM 1316 CG1 VAL A 170 10.500 35.607 −3.335 1.00 22.54 C ATOM 1317 CG2 VAL A 170 11.874 36.134 −5.362 1.00 28.79 C ATOM 1318 N LEU A 171 9.395 33.406 −7.632 1.00 19.61 N ATOM 1319 CA LEU A 171 8.996 33.451 −9.036 1.00 17.49 C ATOM 1320 C LEU A 171 7.615 34.085 −9.147 1.00 17.41 C ATOM 1321 O LEU A 171 6.686 33.667 −8.453 1.00 19.36 O ATOM 1322 CB LEU A 171 8.963 32.047 −9.636 1.00 18.63 C ATOM 1323 CG LEU A 171 10.282 31.276 −9.665 1.00 26.27 C ATOM 1324 CD1 LEU A 171 10.099 29.942 −10.378 1.00 25.23 C ATOM 1325 CD2 LEU A 171 11.364 32.100 −10.339 1.00 22.36 C ATOM 1326 N PRO A 172 7.471 35.094 −10.022 1.00 14.88 N ATOM 1327 CA PRO A 172 6.223 35.853 −10.159 1.00 14.86 C ATOM 1328 C PRO A 172 5.302 35.268 −11.227 1.00 19.81 C ATOM 1329 O PRO A 172 5.760 34.501 −12.068 1.00 19.14 O ATOM 1330 CB PRO A 172 6.715 37.221 −10.627 1.00 20.22 C ATOM 1331 CG PRO A 172 7.938 36.910 −11.435 1.00 18.21 C ATOM 1332 CD PRO A 172 8.543 35.636 −10.880 1.00 14.89 C ATOM 1333 N ASN A 173 4.024 35.633 −11.184 1.00 22.85 N ATOM 1334 CA ASN A 173 3.073 35.266 −12.235 1.00 29.29 C ATOM 1335 C ASN A 173 3.027 33.769 −12.528 1.00 31.64 C ATOM 1336 O ASN A 173 2.795 33.356 −13.665 1.00 39.41 O ATOM 1337 CB ASN A 173 3.386 36.033 −13.520 1.00 32.47 C ATOM 1338 CG ASN A 173 3.475 37.531 −13.296 1.00 85.40 C ATOM 1339 OD1 ASN A 173 4.280 38.218 −13.926 1.00 59.68 O ATOM 1340 ND2 ASN A 173 2.652 38.044 −12.388 1.00 49.78 N ATOM 1341 N LEU A 174 3.262 32.962 −11.499 1.00 20.60 N ATOM 1342 CA LEU A 174 3.201 31.512 −11.623 1.00 18.27 C ATOM 1343 C LEU A 174 2.155 30.946 −10.685 1.00 25.26 C ATOM 1344 O LEU A 174 2.226 31.128 −9.472 1.00 24.16 O ATOM 1345 CB LEU A 174 4.550 30.872 −11.296 1.00 24.24 C ATOM 1346 CG LEU A 174 5.479 30.472 −12.438 1.00 55.63 C ATOM 1347 CD1 LEU A 174 6.625 29.655 −11.870 1.00 27.72 C ATOM 1348 CD2 LEU A 174 4.722 29.681 −13.495 1.00 33.38 C ATOM 1349 N SER A 175 1.178 30.253 −11.247 1.00 19.56 N ATOM 1350 CA SER A 175 0.212 29.552 −10.427 1.00 21.54 C ATOM 1351 C SER A 175 0.218 28.100 −10.855 1.00 20.84 C ATOM 1352 O SER A 175 0.958 27.711 −11.761 1.00 18.86 O ATOM 1353 CB SER A 175 −1.182 30.157 −10.597 1.00 21.73 C ATOM 1354 OG SER A 175 −1.679 29.929 −11.903 1.00 27.11 O ATOM 1355 N SER A 176 −0.599 27.294 −10.192 1.00 16.51 N ATOM 1356 CA SER A 176 −0.839 25.940 −10.640 1.00 17.04 C ATOM 1357 C SER A 176 −1.830 26.028 −11.798 1.00 16.54 C ATOM 1358 CB SER A 176 −1.400 25.104 −9.485 1.00 17.23 C ATOM 1359 OG SER A 176 −1.399 23.728 −9.797 1.00 20.69 O ATOM 1360 O SER A 176 −2.331 27.110 −12.112 1.00 18.57 O ATOM 1361 N GLY A 177 −2.104 24.904 −12.451 1.00 17.84 N ATOM 1362 CA GLY A 177 −3.036 24.906 −13.564 1.00 18.83 C ATOM 1363 C GLY A 177 −4.467 25.206 −13.144 1.00 14.12 C ATOM 1364 O GLY A 177 −4.815 25.120 −11.960 1.00 14.14 O ATOM 1365 N PRO A 178 −5.312 25.585 −14.105 1.00 13.09 N ATOM 1366 CA PRO A 178 −6.729 25.736 −13.773 1.00 11.60 C ATOM 1367 C PRO A 178 −7.390 24.370 −13.676 1.00 12.12 C ATOM 1368 CB PRO A 178 −7.290 26.513 −14.962 1.00 13.40 C ATOM 1369 CG PRO A 178 −6.386 26.154 −16.109 1.00 22.97 C ATOM 1370 CD PRO A 178 −5.029 25.841 −15.532 1.00 16.39 C ATOM 1371 O PRO A 178 −6.763 23.345 −13.972 1.00 14.28 O ATOM 1372 N ILE A 179 −8.640 24.359 −13.244 1.00 11.60 N ATOM 1373 CA ILE A 179 −9.404 23.126 −13.199 1.00 11.12 C ATOM 1374 C ILE A 179 −9.693 22.662 −14.633 1.00 13.21 C ATOM 1375 O ILE A 179 −10.218 23.434 −15.444 1.00 14.90 O ATOM 1376 CB ILE A 179 −10.707 23.357 −12.430 1.00 10.34 C ATOM 1377 CG1 ILE A 179 −10.392 23.610 −10.955 1.00 14.08 C ATOM 1378 CG2 ILE A 179 −11.661 22.179 −12.590 1.00 14.20 C ATOM 1379 CD1 ILE A 179 −11.518 24.273 −10.208 1.00 12.85 C ATOM 1380 N ASP A 180 −9.324 21.421 −14.957 1.00 12.91 N ATOM 1381 CA ASP A 180 −9.567 20.876 −16.302 1.00 10.51 C ATOM 1382 C ASP A 180 −10.792 19.985 −16.253 1.00 10.15 C ATOM 1383 O ASP A 180 −10.707 18.794 −15.928 1.00 12.02 O ATOM 1384 CB ASP A 180 −8.352 20.098 −16.819 1.00 15.37 C ATOM 1385 CG ASP A 180 −8.568 19.517 −18.225 1.00 13.01 C ATOM 1386 OD1 ASP A 180 −9.687 19.646 −18.779 1.00 13.99 O ATOM 1387 OD2 ASP A 180 −7.603 18.924 −18.759 1.00 17.65 O ATOM 1388 N SER A 181 −11.938 20.570 −16.553 1.00 10.15 N ATOM 1389 CA SER A 181 −13.199 19.873 −16.436 1.00 8.88 C ATOM 1390 C SER A 181 −13.310 18.686 −17.396 1.00 8.77 C ATOM 1391 O SER A 181 −14.090 17.763 −17.151 1.00 9.07 O ATOM 1392 CB SER A 181 −14.345 20.842 −16.676 1.00 9.62 C ATOM 1393 OG SER A 181 −14.145 21.506 −17.921 1.00 11.79 O ATOM 1394 N SER A 182 −12.554 18.727 −18.494 1.00 8.53 N ATOM 1395 CA SER A 182 −12.675 17.689 −19.518 1.00 8.81 C ATOM 1396 C SER A 182 −12.171 16.328 −19.032 1.00 9.43 C ATOM 1397 O SER A 182 −12.534 15.295 −19.607 1.00 11.89 O ATOM 1398 CB SER A 182 −11.943 18.093 −20.807 1.00 10.60 C ATOM 1399 OG SER A 182 −10.552 17.939 −20.670 1.00 14.76 O ATOM 1400 N VAL A 183 −11.337 16.319 −17.996 1.00 8.40 N ATOM 1401 CA VAL A 183 −10.853 15.054 −17.451 1.00 9.30 C ATOM 1402 C VAL A 183 −11.542 14.715 −16.136 1.00 7.84 C ATOM 1403 O VAL A 183 −11.115 13.791 −15.443 1.00 9.46 O ATOM 1404 CB VAL A 183 −9.327 15.039 −17.257 1.00 9.77 C ATOM 1405 CG1 VAL A 183 −8.625 15.275 −18.591 1.00 13.98 C ATOM 1406 CG2 VAL A 183 −8.889 16.064 −16.216 1.00 12.72 C ATOM 1407 N LEU A 184 −12.597 15.457 −15.809 1.00 6.49 N ATOM 1408 CA LEU A 184 −13.291 15.282 −14.531 1.00 7.18 C ATOM 1409 C LEU A 184 −14.721 14.767 −14.699 1.00 8.94 C ATOM 1410 O LEU A 184 −15.369 14.390 −13.728 1.00 7.03 O ATOM 1411 CB LEU A 184 −13.225 16.574 −13.686 1.00 7.27 C ATOM 1412 CG LEU A 184 −11.797 17.033 −13.382 1.00 5.81 C ATOM 1413 CD1 LEU A 184 −11.784 18.379 −12.656 1.00 8.64 C ATOM 1414 CD2 LEU A 184 −11.033 15.993 −12.570 1.00 8.78 C ATOM 1415 N SER A 185 −15.217 14.731 −15.934 1.00 6.60 N ATOM 1416 CA SER A 185 −16.447 14.011 −16.253 1.00 8.04 C ATOM 1417 C SER A 185 −16.374 13.507 −17.684 1.00 9.06 C ATOM 1418 O SER A 185 −15.879 14.221 −18.562 1.00 9.74 O ATOM 1419 CB SER A 185 −17.690 14.892 −16.123 1.00 7.37 C ATOM 1420 OG SER A 185 −18.831 14.192 −16.585 1.00 7.90 O ATOM 1421 N ARG A 186 −16.913 12.318 −17.932 1.00 7.99 N ATOM 1422 CA ARG A 186 −16.986 11.784 −19.296 1.00 8.17 C ATOM 1423 C ARG A 186 −18.178 12.352 −20.056 1.00 11.97 C ATOM 1424 O ARG A 186 −18.309 12.136 −21.264 1.00 11.61 O ATOM 1425 CB ARG A 186 −17.057 10.250 −19.272 1.00 10.81 C ATOM 1426 CG ARG A 186 −15.777 9.591 −18.788 1.00 10.26 C ATOM 1427 CD ARG A 186 −15.960 8.081 −18.583 1.00 10.74 C ATOM 1428 NE ARG A 186 −17.037 7.816 −17.635 1.00 10.08 N ATOM 1429 CZ ARG A 186 −17.587 6.622 −17.426 1.00 13.38 C ATOM 1430 NH1 ARG A 186 −17.149 5.566 −18.108 1.00 14.05 N ATOM 1431 NH2 ARG A 186 −18.572 6.479 −16.551 1.00 12.05 N ATOM 1432 N ASN A 187 −19.062 13.055 −19.358 1.00 8.13 N ATOM 1433 CA ASN A 187 −20.254 13.610 −19.978 1.00 8.18 C ATOM 1434 C ASN A 187 −19.929 14.967 −20.601 1.00 10.33 C ATOM 1435 O ASN A 187 −19.820 15.977 −19.899 1.00 9.28 O ATOM 1436 CB ASN A 187 −21.383 13.720 −18.943 1.00 7.71 C ATOM 1437 CG ASN A 187 −22.700 14.159 −19.548 1.00 8.65 C ATOM 1438 OD1 ASN A 187 −22.731 14.989 −20.462 1.00 10.78 O ATOM 1439 ND2 ASN A 187 −23.797 13.613 −19.046 1.00 11.01 N ATOM 1440 N LYS A 188 −19.750 14.982 −21.918 1.00 10.09 N ATOM 1441 CA LYS A 188 −19.290 16.182 −22.611 1.00 10.45 C ATOM 1442 C LYS A 188 −20.274 17.335 −22.497 1.00 8.22 C ATOM 1443 O LYS A 188 −19.854 18.498 −22.440 1.00 10.20 O ATOM 1444 CB LYS A 188 −18.984 15.865 −24.079 1.00 12.84 C ATOM 1445 CG LYS A 188 −17.682 15.087 −24.242 1.00 16.21 C ATOM 1446 CD LYS A 188 −17.316 14.886 −25.702 1.00 30.25 C ATOM 1447 CE LYS A 188 −17.788 13.538 −26.215 1.00 59.11 C ATOM 1448 NZ LYS A 188 −16.968 12.425 −25.656 1.00 62.44 N ATOM 1449 N THR A 189 −21.558 17.018 −22.461 1.00 8.16 N ATOM 1450 CA THR A 189 −22.590 18.029 −22.287 1.00 9.52 C ATOM 1451 C THR A 189 −22.440 18.716 −20.921 1.00 11.14 C ATOM 1452 O THR A 189 −22.499 19.947 −20.822 1.00 10.76 O ATOM 1453 CB THR A 189 −24.002 17.422 −22.419 1.00 11.47 C ATOM 1454 OG1 THR A 189 −24.083 16.672 −23.641 1.00 21.86 O ATOM 1455 CG2 THR A 189 −25.069 18.514 −22.442 1.00 15.48 C ATOM 1456 N GLU A 190 −22.243 17.917 −19.866 1.00 7.70 N ATOM 1457 CA GLU A 190 −22.042 18.473 −18.525 1.00 6.48 C ATOM 1458 C GLU A 190 −20.762 19.295 −18.456 1.00 6.09 C ATOM 1459 O GLU A 190 −20.723 20.327 −17.779 1.00 7.57 O ATOM 1460 CB GLU A 190 −22.047 17.360 −17.468 1.00 7.78 C ATOM 1461 CG GLU A 190 −23.387 16.671 −17.321 1.00 10.63 C ATOM 1462 CD GLU A 190 −24.469 17.574 −16.735 1.00 19.84 C ATOM 1463 OE1 GLU A 190 −24.149 18.687 −16.262 1.00 14.70 O ATOM 1464 OE2 GLU A 190 −25.650 17.164 −16.743 1.00 48.07 O ATOM 1465 N VAL A 191 −19.709 18.864 −19.139 1.00 6.34 N ATOM 1466 CA VAL A 191 −18.481 19.653 −19.206 1.00 7.23 C ATOM 1467 C VAL A 191 −18.752 21.037 −19.820 1.00 9.26 C ATOM 1468 O VAL A 191 −18.303 22.054 −19.289 1.00 8.62 O ATOM 1469 CB VAL A 191 −17.369 18.914 −19.990 1.00 7.21 C ATOM 1470 CG1 VAL A 191 −16.176 19.816 −20.252 1.00 10.02 C ATOM 1471 CG2 VAL A 191 −16.945 17.649 −19.229 1.00 9.40 C ATOM 1472 N ASP A 192 −19.496 21.067 −20.924 1.00 8.63 N ATOM 1473 CA ASP A 192 −19.794 22.326 −21.601 1.00 9.12 C ATOM 1474 C ASP A 192 −20.662 23.232 −20.723 1.00 7.92 C ATOM 1475 O ASP A 192 −20.481 24.456 −20.705 1.00 8.58 O ATOM 1476 CB ASP A 192 −20.505 22.061 −22.930 1.00 8.58 C ATOM 1477 CG ASP A 192 −19.550 21.589 −24.026 1.00 12.97 C ATOM 1478 OD1 ASP A 192 −18.343 21.894 −23.950 1.00 19.09 O ATOM 1479 OD2 ASP A 192 −20.020 20.912 −24.968 1.00 13.65 O ATOM 1480 N ILE A 193 −21.614 22.636 −20.014 1.00 6.50 N ATOM 1481 CA ILE A 193 −22.479 23.391 −19.111 1.00 6.64 C ATOM 1482 C ILE A 193 −21.658 24.019 −17.992 1.00 8.30 C ATOM 1483 O ILE A 193 −21.797 25.211 −17.684 1.00 9.16 O ATOM 1484 CB ILE A 193 −23.594 22.499 −18.555 1.00 6.90 C ATOM 1485 CG1 ILE A 193 −24.608 22.219 −19.667 1.00 9.28 C ATOM 1486 CG2 ILE A 193 −24.291 23.153 −17.355 1.00 9.32 C ATOM 1487 CD1 ILE A 193 −25.635 21.164 −19.323 1.00 11.81 C ATOM 1488 N TYR A 194 −20.766 23.230 −17.403 1.00 6.21 N ATOM 1489 CA TYR A 194 −19.902 23.749 −16.359 1.00 6.09 C ATOM 1490 C TYR A 194 −19.037 24.896 −16.880 1.00 6.70 C ATOM 1491 O TYR A 194 −18.930 25.955 −16.238 1.00 7.31 O ATOM 1492 CB TYR A 194 −19.023 22.623 −15.814 1.00 6.50 C ATOM 1493 CG TYR A 194 −17.954 23.098 −14.861 1.00 6.88 C ATOM 1494 CD1 TYR A 194 −18.239 23.297 −13.501 1.00 7.46 C ATOM 1495 CD2 TYR A 194 −16.670 23.355 −15.305 1.00 6.99 C ATOM 1496 CE1 TYR A 194 −17.254 23.734 −12.635 1.00 6.75 C ATOM 1497 CE2 TYR A 194 −15.681 23.774 −14.445 1.00 8.92 C ATOM 1498 CZ TYR A 194 −15.981 23.965 −13.105 1.00 7.57 C ATOM 1499 OH TYR A 194 −14.961 24.384 −12.276 1.00 11.18 O ATOM 1500 N ASN A 195 −18.401 24.688 −18.028 1.00 6.89 N ATOM 1501 CA ASN A 195 −17.462 25.666 −18.552 1.00 8.53 C ATOM 1502 C ASN A 195 −18.103 27.032 −18.812 1.00 8.54 C ATOM 1503 O ASN A 195 −17.411 28.044 −18.744 1.00 10.97 O ATOM 1504 CB ASN A 195 −16.820 25.175 −19.856 1.00 8.26 C ATOM 1505 CG ASN A 195 −15.794 24.074 −19.648 1.00 13.25 C ATOM 1506 OD1 ASN A 195 −15.364 23.433 −20.610 1.00 14.63 O ATOM 1507 ND2 ASN A 195 −15.385 23.861 −18.416 1.00 9.36 N ATOM 1508 N SER A 196 −19.388 27.069 −19.120 1.00 6.92 N ATOM 1509 CA ASER A 196 −20.047 28.337 −19.432 0.35 8.60 C ATOM 1510 C SER A 196 −20.869 28.885 −18.264 1.00 8.11 C ATOM 1511 O SER A 196 −21.634 29.832 −18.424 1.00 8.53 O ATOM 1512 CB ASER A 196 −20.917 28.198 −20.679 0.35 15.69 C ATOM 1513 OG ASER A 196 −21.879 27.180 −20.503 0.35 10.54 O ATOM 1514 CA BSER A 196 −20.047 28.337 −19.432 0.35 8.84 C ATOM 1515 CB BSER A 196 −20.917 28.198 −20.679 0.35 15.69 C ATOM 1516 OG BSER A 196 −21.878 27.179 −20.504 0.35 10.54 O ATOM 1517 CA CSER A 196 −20.030 28.350 −19.424 0.30 7.88 C ATOM 1518 CB CSER A 196 −20.829 28.311 −20.741 0.30 17.42 C ATOM 1519 OG CSER A 196 −21.208 26.999 −21.123 0.30 5.94 O ATOM 1520 N ASP A 197 −20.712 28.283 −17.088 1.00 7.36 N ATOM 1521 CA ASP A 197 −21.378 28.788 −15.890 1.00 7.39 C ATOM 1522 C ASP A 197 −20.675 30.091 −15.452 1.00 5.11 C ATOM 1523 O ASP A 197 −19.472 30.105 −15.231 1.00 7.19 O ATOM 1524 CB ASP A 197 −21.307 27.710 −14.799 1.00 7.00 C ATOM 1525 CG ASP A 197 −22.001 28.111 −13.506 1.00 12.88 C ATOM 1526 OD1 ASP A 197 −22.176 29.315 −13.216 1.00 9.53 O ATOM 1527 OD2 ASP A 197 −22.354 27.193 −12.734 1.00 9.68 O ATOM 1528 N PRO A 198 −21.441 31.197 −15.362 1.00 7.84 N ATOM 1529 CA PRO A 198 −20.779 32.480 −15.077 1.00 8.09 C ATOM 1530 C PRO A 198 −20.238 32.580 −13.644 1.00 9.46 C ATOM 1531 O PRO A 198 −19.519 33.532 −13.335 1.00 12.16 O ATOM 1532 CB PRO A 198 −21.895 33.517 −15.282 1.00 8.81 C ATOM 1533 CG PRO A 198 −23.166 32.783 −15.271 1.00 12.52 C ATOM 1534 CD PRO A 198 −22.891 31.321 −15.544 1.00 8.16 C ATOM 1535 N LEU A 199 −20.561 31.604 −12.796 1.00 7.46 N ATOM 1536 CA LEU A 199 −20.220 31.683 −11.372 1.00 10.37 C ATOM 1537 C LEU A 199 −19.048 30.798 −10.951 1.00 12.05 C ATOM 1538 O LEU A 199 −18.687 30.775 −9.763 1.00 11.02 O ATOM 1539 CB LEU A 199 −21.451 31.367 −10.526 1.00 7.80 C ATOM 1540 CG LEU A 199 −22.611 32.350 −10.675 1.00 10.76 C ATOM 1541 CD1 LEU A 199 −23.818 31.905 −9.861 1.00 11.32 C ATOM 1542 CD2 LEU A 199 −22.164 33.760 −10.266 1.00 14.15 C ATOM 1543 N ILE A 200 −18.459 30.065 −11.895 1.00 8.07 N ATOM 1544 CA ILE A 200 −17.275 29.255 −11.599 1.00 6.42 C ATOM 1545 C ILE A 200 −16.006 30.084 −11.705 1.00 7.71 C ATOM 1546 O ILE A 200 −16.051 31.229 −12.184 1.00 12.31 O ATOM 1547 CB ILE A 200 −17.172 28.017 −12.531 1.00 7.22 C ATOM 1548 CG1 ILE A 200 −16.906 28.441 −13.992 1.00 10.03 C ATOM 1549 CG2 ILE A 200 −18.421 27.151 −12.401 1.00 8.89 C ATOM 1550 CD1 ILE A 200 −16.361 27.315 −14.869 1.00 10.39 C ATOM 1551 N CYS A 201 −14.875 29.524 −11.293 1.00 7.95 N ATOM 1552 CA CYS A 201 −13.587 30.182 −11.468 1.00 9.49 C ATOM 1553 C CYS A 201 −12.723 29.352 −12.404 1.00 13.48 C ATOM 1554 O CYS A 201 −12.434 28.187 −12.106 1.00 13.84 O ATOM 1555 CB CYS A 201 −12.870 30.343 −10.125 1.00 12.53 C ATOM 1556 SG CYS A 201 −11.270 31.173 −10.289 1.00 17.94 S ATOM 1557 N ARG A 202 −12.303 29.959 −13.515 1.00 11.34 N ATOM 1558 CA ARG A 202 −11.533 29.264 −14.554 1.00 11.13 C ATOM 1559 C ARG A 202 −10.064 29.653 −14.550 1.00 12.74 C ATOM 1560 O ARG A 202 −9.317 29.269 −15.449 1.00 14.37 O ATOM 1561 CB ARG A 202 −12.123 29.558 −15.936 1.00 12.12 C ATOM 1562 CG ARG A 202 −13.617 29.317 −16.013 1.00 15.07 C ATOM 1563 CD ARG A 202 −14.121 29.443 −17.439 1.00 19.32 C ATOM 1564 NE ARG A 202 −13.749 28.272 −18.222 1.00 18.70 N ATOM 1565 CZ ARG A 202 −13.869 28.184 −19.543 1.00 26.00 C ATOM 1566 NH1 ARG A 202 −14.349 29.207 −20.236 1.00 22.12 N ATOM 1567 NH2 ARG A 202 −13.509 27.071 −20.166 1.00 19.47 N ATOM 1568 N ALA A 203 −9.646 30.408 −13.538 1.00 12.06 N ATOM 1569 CA ALA A 203 −8.263 30.859 −13.438 1.00 13.49 C ATOM 1570 C ALA A 203 −7.346 29.766 −12.897 1.00 12.80 C ATOM 1571 O ALA A 203 −7.812 28.796 −12.294 1.00 12.79 O ATOM 1572 CB ALA A 203 −8.180 32.109 −12.557 1.00 16.80 C ATOM 1573 N GLY A 204 −6.043 29.919 −13.104 1.00 12.71 N ATOM 1574 CA GLY A 204 −5.083 29.005 −12.518 1.00 13.49 C ATOM 1575 C GLY A 204 −5.213 29.001 −11.006 1.00 14.76 C ATOM 1576 O GLY A 204 −5.478 30.037 −10.395 1.00 14.87 O ATOM 1577 N LEU A 205 −5.053 27.838 −10.394 1.00 12.15 N ATOM 1578 CA ALEU A 205 −5.099 27.763 −8.938 0.50 12.52 C ATOM 1579 C LEU A 205 −3.877 28.430 −8.323 1.00 12.12 C ATOM 1580 O LEU A 205 −2.738 28.073 −8.617 1.00 14.37 O ATOM 1581 CB ALEU A 205 −5.233 26.317 −8.455 0.50 21.10 C ATOM 1582 CG ALEU A 205 −6.675 25.832 −8.280 0.50 22.60 C ATOM 1583 CD1 ALEU A 205 −7.347 25.614 −9.629 0.50 46.72 C ATOM 1584 CD2 ALEU A 205 −6.729 24.565 −7.437 0.50 21.86 C ATOM 1585 CA BLEU A 205 −5.093 27.740 −8.941 0.50 14.43 C ATOM 1586 CB BLEU A 205 −5.152 26.271 −8.524 0.50 15.12 C ATOM 1587 CG BLEU A 205 −5.569 25.980 −7.083 0.50 25.82 C ATOM 1588 CD1 BLEU A 205 −6.333 24.666 −6.994 0.50 50.50 C ATOM 1589 CD2 BLEU A 205 −4.358 25.965 −6.180 0.50 39.57 C ATOM 1590 N LYS A 206 −4.119 29.419 −7.467 1.00 10.85 N ATOM 1591 CA LYS A 206 −3.027 30.161 −6.853 1.00 11.66 C ATOM 1592 C LYS A 206 −2.265 29.295 −5.866 1.00 12.14 C ATOM 1593 O LYS A 206 −2.852 28.446 −5.188 1.00 11.48 O ATOM 1594 CB LYS A 206 −3.563 31.409 −6.157 1.00 15.47 C ATOM 1595 CG LYS A 206 −4.079 32.451 −7.138 1.00 20.12 C ATOM 1596 CD LYS A 206 −4.787 33.588 −6.426 1.00 37.03 C ATOM 1597 CE LYS A 206 −5.080 34.727 −7.388 1.00 51.15 C ATOM 1598 NZ LYS A 206 −3.843 35.225 −8.052 1.00 92.27 N ATOM 1599 N VAL A 207 −0.959 29.503 −5.774 1.00 10.91 N ATOM 1600 CA VAL A 207 −0.145 28.709 −4.867 1.00 11.61 C ATOM 1601 C VAL A 207 −0.645 28.809 −3.421 1.00 12.70 C ATOM 1602 O VAL A 207 −0.680 27.816 −2.702 1.00 12.20 O ATOM 1603 CB VAL A 207 1.347 29.092 −4.957 1.00 13.57 C ATOM 1604 CG1 VAL A 207 2.124 28.508 −3.785 1.00 16.27 C ATOM 1605 CG2 VAL A 207 1.918 28.614 −6.280 1.00 15.13 C ATOM 1606 N CYS A 208 −1.043 30.001 −2.988 1.00 10.56 N ATOM 1607 CA CYS A 208 −1.537 30.138 −1.619 1.00 12.51 C ATOM 1608 C CYS A 208 −2.766 29.252 −1.368 1.00 12.06 C ATOM 1609 O CYS A 208 −2.927 28.698 −0.284 1.00 12.63 O ATOM 1610 CB CYS A 208 −1.844 31.602 −1.287 1.00 13.86 C ATOM 1611 SG CYS A 208 −3.147 32.334 −2.291 1.00 19.08 S ATOM 1612 N PHE A 209 −3.620 29.107 −2.378 1.00 10.09 N ATOM 1613 CA PHE A 209 −4.827 28.297 −2.226 1.00 10.18 C ATOM 1614 C PHE A 209 −4.474 26.817 −2.261 1.00 9.52 C ATOM 1615 O PHE A 209 −4.999 26.045 −1.466 1.00 9.70 O ATOM 1616 CB PHE A 209 −5.862 28.632 −3.298 1.00 8.96 C ATOM 1617 CG PHE A 209 −7.213 28.020 −3.047 1.00 10.85 C ATOM 1618 CD1 PHE A 209 −7.979 28.421 −1.965 1.00 15.24 C ATOM 1619 CD2 PHE A 209 −7.721 27.055 −3.904 1.00 11.35 C ATOM 1620 CE1 PHE A 209 −9.230 27.863 −1.737 1.00 19.47 C ATOM 1621 CE2 PHE A 209 −8.967 26.493 −3.680 1.00 13.97 C ATOM 1622 CZ PHE A 209 −9.722 26.901 −2.603 1.00 16.68 C ATOM 1623 N GLY A 210 −3.596 26.423 −3.179 1.00 10.17 N ATOM 1624 CA GLY A 210 −3.119 25.054 −3.215 1.00 10.27 C ATOM 1625 C GLY A 210 −2.529 24.619 −1.887 1.00 9.64 C ATOM 1626 O GLY A 210 −2.727 23.483 −1.453 1.00 10.94 O ATOM 1627 N ILE A 211 −1.798 25.525 −1.246 1.00 9.76 N ATOM 1628 CA ILE A 211 −1.219 25.237 0.060 1.00 10.73 C ATOM 1629 C ILE A 211 −2.334 24.946 1.064 1.00 9.63 C ATOM 1630 O ILE A 211 −2.225 24.023 1.872 1.00 11.27 O ATOM 1631 CB ILE A 211 −0.326 26.394 0.547 1.00 10.51 C ATOM 1632 CG1 ILE A 211 0.968 26.424 −0.264 1.00 14.10 C ATOM 1633 CG2 ILE A 211 −0.019 26.260 2.051 1.00 15.16 C ATOM 1634 CD1 ILE A 211 1.777 27.688 −0.060 1.00 19.74 C ATOM 1635 N GLN A 212 −3.415 25.716 0.999 1.00 8.87 N ATOM 1636 CA GLN A 212 −4.550 25.457 1.887 1.00 9.46 C ATOM 1637 C GLN A 212 −5.228 24.114 1.579 1.00 10.55 C ATOM 1638 O GLN A 212 −5.725 23.448 2.492 1.00 10.09 O ATOM 1639 CB GLN A 212 −5.549 26.618 1.865 1.00 8.41 C ATOM 1640 CG GLN A 212 −4.979 27.899 2.496 1.00 9.42 C ATOM 1641 CD GLN A 212 −4.434 27.662 3.902 1.00 10.45 C ATOM 1642 OE1 GLN A 212 −5.011 26.906 4.686 1.00 11.66 O ATOM 1643 NE2 GLN A 212 −3.323 28.311 4.222 1.00 14.57 N ATOM 1644 N LEU A 213 −5.241 23.704 0.306 1.00 9.40 N ATOM 1645 CA LEU A 213 −5.764 22.378 −0.036 1.00 10.49 C ATOM 1646 C LEU A 213 −4.854 21.266 0.505 1.00 9.28 C ATOM 1647 O LEU A 213 −5.343 20.236 0.962 1.00 10.04 O ATOM 1648 CB LEU A 213 −5.973 22.236 −1.546 1.00 9.58 C ATOM 1649 CG LEU A 213 −7.050 23.140 −2.143 1.00 10.05 C ATOM 1650 CD1 LEU A 213 −7.097 22.976 −3.663 1.00 14.31 C ATOM 1651 CD2 LEU A 213 −8.407 22.838 −1.528 1.00 14.79 C ATOM 1652 N LEU A 214 −3.541 21.477 0.478 1.00 9.43 N ATOM 1653 CA LEU A 214 −2.616 20.540 1.123 1.00 11.38 C ATOM 1654 C LEU A 214 −2.855 20.488 2.634 1.00 11.40 C ATOM 1655 O LEU A 214 −2.800 19.411 3.249 1.00 11.93 O ATOM 1656 CB LEU A 214 −1.157 20.914 0.856 1.00 12.30 C ATOM 1657 CG LEU A 214 −0.639 20.817 −0.582 1.00 17.43 C ATOM 1658 CD1 LEU A 214 0.811 21.288 −0.643 1.00 17.60 C ATOM 1659 CD2 LEU A 214 −0.764 19.397 −1.091 1.00 18.65 C ATOM 1660 N ASN A 215 −3.105 21.650 3.234 1.00 10.49 N ATOM 1661 CA ASN A 215 −3.460 21.701 4.651 1.00 11.90 C ATOM 1662 C ASN A 215 −4.717 20.879 4.909 1.00 10.86 C ATOM 1663 O ASN A 215 −4.788 20.130 5.884 1.00 12.49 O ATOM 1664 CB ASN A 215 −3.696 23.143 5.109 1.00 9.81 C ATOM 1665 CG ASN A 215 −2.413 23.943 5.231 1.00 13.81 C ATOM 1666 OD1 ASN A 215 −1.309 23.393 5.195 1.00 15.52 O ATOM 1667 ND2 ASN A 215 −2.556 25.257 5.381 1.00 15.57 N ATOM 1668 N ALA A 216 −5.709 21.009 4.031 1.00 9.70 N ATOM 1669 CA ALA A 216 −6.940 20.245 4.172 1.00 10.39 C ATOM 1670 C ALA A 216 −6.662 18.742 4.172 1.00 11.63 C ATOM 1671 O ALA A 216 −7.177 18.013 5.021 1.00 11.59 O ATOM 1672 CB ALA A 216 −7.942 20.617 3.078 1.00 11.90 C ATOM 1673 N VAL A 217 −5.856 18.282 3.217 1.00 11.05 N ATOM 1674 CA VAL A 217 −5.522 16.864 3.131 1.00 12.23 C ATOM 1675 C VAL A 217 −4.844 16.383 4.417 1.00 11.43 C ATOM 1676 O VAL A 217 −5.205 15.340 4.961 1.00 11.37 O ATOM 1677 CB VAL A 217 −4.642 16.575 1.898 1.00 12.66 C ATOM 1678 CG1 VAL A 217 −4.053 15.157 1.955 1.00 15.90 C ATOM 1679 CG2 VAL A 217 −5.449 16.780 0.618 1.00 13.74 C ATOM 1680 N SER A 218 −3.884 17.155 4.910 1.00 10.49 N ATOM 1681 CA ASER A 218 −3.194 16.822 6.152 0.50 11.81 C ATOM 1682 C SER A 218 −4.174 16.752 7.322 1.00 12.18 C ATOM 1683 O SER A 218 −4.142 15.814 8.127 1.00 13.97 O ATOM 1684 CB ASER A 218 −2.103 17.853 6.442 0.50 15.09 C ATOM 1685 OG ASER A 218 −1.031 17.731 5.527 0.50 17.82 O ATOM 1686 CA BSER A 218 −3.194 16.811 6.151 0.50 10.96 C ATOM 1687 CB BSER A 218 −2.072 17.812 6.439 0.50 14.67 C ATOM 1688 OG BSER A 218 −1.434 17.523 7.675 0.50 19.05 O ATOM 1689 N ARG A 219 −5.054 17.740 7.415 1.00 9.30 N ATOM 1690 CA ARG A 219 −6.019 17.783 8.511 1.00 11.05 C ATOM 1691 C ARG A 219 −7.045 16.657 8.422 1.00 10.10 C ATOM 1692 O ARG A 219 −7.451 16.091 9.439 1.00 10.71 O ATOM 1693 CB ARG A 219 −6.700 19.152 8.579 1.00 10.50 C ATOM 1694 CG ARG A 219 −5.708 20.260 8.925 1.00 10.95 C ATOM 1695 CD ARG A 219 −6.290 21.639 8.732 1.00 13.38 C ATOM 1696 NE ARG A 219 −5.238 22.651 8.755 1.00 13.54 N ATOM 1697 CZ ARG A 219 −5.455 23.955 8.635 1.00 12.88 C ATOM 1698 NH1 ARG A 219 −6.690 24.413 8.499 1.00 12.45 N ATOM 1699 NH2 ARG A 219 −4.427 24.797 8.662 1.00 14.24 N ATOM 1700 N VAL A 220 −7.466 16.320 7.206 1.00 9.48 N ATOM 1701 CA VAL A 220 −8.391 15.216 7.021 1.00 10.61 C ATOM 1702 C VAL A 220 −7.758 13.921 7.526 1.00 10.79 C ATOM 1703 O VAL A 220 −8.403 13.143 8.223 1.00 11.64 O ATOM 1704 CB VAL A 220 −8.834 15.084 5.547 1.00 9.99 C ATOM 1705 CG1 VAL A 220 −9.476 13.727 5.296 1.00 10.95 C ATOM 1706 CG2 VAL A 220 −9.802 16.210 5.190 1.00 11.57 C ATOM 1707 N GLU A 221 −6.489 13.706 7.198 1.00 13.35 N ATOM 1708 CA GLU A 221 −5.800 12.492 7.633 1.00 14.85 C ATOM 1709 C GLU A 221 −5.815 12.368 9.157 1.00 18.26 C ATOM 1710 O GLU A 221 −6.082 11.295 9.701 1.00 18.73 O ATOM 1711 CB GLU A 221 −4.362 12.481 7.115 1.00 18.69 C ATOM 1712 CG GLU A 221 −3.543 11.285 7.574 1.00 51.12 C ATOM 1713 CD GLU A 221 −2.103 11.354 7.102 1.00 92.75 C ATOM 1714 OE1 GLU A 221 −1.704 12.403 6.551 1.00 79.10 O ATOM 1715 OE2 GLU A 221 −1.369 10.358 7.283 1.00 103.53 O ATOM 1716 N ARG A 222 −5.545 13.473 9.844 1.00 14.30 N ATOM 1717 CA ARG A 222 −5.568 13.479 11.305 1.00 15.32 C ATOM 1718 C ARG A 222 −6.967 13.282 11.865 1.00 13.43 C ATOM 1719 O ARG A 222 −7.139 12.698 12.936 1.00 19.93 O ATOM 1720 CB ARG A 222 −4.954 14.774 11.853 1.00 20.09 C ATOM 1721 CG ARG A 222 −3.440 14.809 11.778 1.00 30.84 C ATOM 1722 CD ARG A 222 −2.868 16.013 12.513 1.00 36.59 C ATOM 1723 NE ARG A 222 −3.115 17.262 11.798 1.00 51.40 N ATOM 1724 CZ ARG A 222 −2.332 17.740 10.837 1.00 65.64 C ATOM 1725 NH1 ARG A 222 −1.245 17.073 10.471 1.00 72.52 N ATOM 1726 NH2 ARG A 222 −2.635 18.885 10.240 1.00 34.72 N ATOM 1727 N ALA A 223 −7.971 13.770 11.149 1.00 12.61 N ATOM 1728 CA ALA A 223 −9.345 13.670 11.607 1.00 14.25 C ATOM 1729 C ALA A 223 −9.941 12.264 11.444 1.00 14.35 C ATOM 1730 O ALA A 223 −10.856 11.894 12.178 1.00 17.85 O ATOM 1731 CB ALA A 223 −10.211 14.692 10.886 1.00 15.85 C ATOM 1732 N LEU A 224 −9.429 11.502 10.476 1.00 14.85 N ATOM 1733 CA LEU A 224 −10.055 10.231 10.085 1.00 19.59 C ATOM 1734 C LEU A 224 −10.274 9.268 11.252 1.00 18.08 C ATOM 1735 O LEU A 224 −11.392 8.799 11.455 1.00 21.08 O ATOM 1736 CB LEU A 224 −9.277 9.537 8.958 1.00 18.13 C ATOM 1737 CG LEU A 224 −9.303 10.188 7.572 1.00 21.40 C ATOM 1738 CD1 LEU A 224 −8.687 9.260 6.531 1.00 28.66 C ATOM 1739 CD2 LEU A 224 −10.712 10.584 7.173 1.00 23.13 C ATOM 1740 N PRO A 225 −9.213 8.985 12.031 1.00 23.78 N ATOM 1741 CA PRO A 225 −9.334 8.027 13.138 1.00 24.17 C ATOM 1742 C PRO A 225 −10.310 8.479 14.215 1.00 26.85 C ATOM 1743 O PRO A 225 −10.636 7.694 15.106 1.00 34.94 O ATOM 1744 CB PRO A 225 −7.915 7.974 13.713 1.00 28.13 C ATOM 1745 CG PRO A 225 −7.034 8.443 12.608 1.00 36.69 C ATOM 1746 CD PRO A 225 −7.833 9.477 11.884 1.00 20.63 C ATOM 1747 N LYS A 226 −10.771 9.723 14.130 1.00 25.36 N ATOM 1748 CA LYS A 226 −11.684 10.280 15.120 1.00 25.72 C ATOM 1749 C LYS A 226 −13.132 10.300 14.630 1.00 33.01 C ATOM 1750 O LYS A 226 −14.058 10.524 15.408 1.00 28.49 O ATOM 1751 CB LYS A 226 −11.248 11.700 15.486 1.00 44.44 C ATOM 1752 CG LYS A 226 −9.761 11.834 15.776 1.00 42.51 C ATOM 1753 CD LYS A 226 −9.371 13.289 15.988 1.00 69.34 C ATOM 1754 CE LYS A 226 −7.876 13.432 16.224 1.00 70.90 C ATOM 1755 NZ LYS A 226 −7.485 14.853 16.441 1.00 84.95 N ATOM 1756 N LEU A 227 −13.318 10.062 13.336 1.00 20.18 N ATOM 1757 CA ALEU A 227 −14.637 10.116 12.716 0.50 15.98 C ATOM 1758 C LEU A 227 −15.525 8.981 13.183 1.00 13.40 C ATOM 1759 O LEU A 227 −15.109 7.818 13.166 1.00 17.01 O ATOM 1760 CB ALEU A 227 −14.512 10.017 11.196 0.50 17.93 C ATOM 1761 CG ALEU A 227 −14.149 11.259 10.394 0.50 13.32 C ATOM 1762 CD1 ALEU A 227 −14.050 10.874 8.923 0.50 13.43 C ATOM 1763 CD2 ALEU A 227 −15.179 12.355 10.601 0.50 15.66 C ATOM 1764 CA BLEU A 227 −14.632 10.132 12.717 0.50 15.66 C ATOM 1765 CB BLEU A 227 −14.470 10.100 11.192 0.50 18.07 C ATOM 1766 CG BLEU A 227 −15.573 10.629 10.274 0.50 15.22 C ATOM 1767 CD1 BLEU A 227 −15.891 12.088 10.568 0.50 24.87 C ATOM 1768 CD2 BLEU A 227 −15.155 10.453 8.822 0.50 11.89 C ATOM 1769 N THR A 228 −16.746 9.311 13.596 1.00 10.05 N ATOM 1770 CA THR A 228 −17.727 8.299 13.997 1.00 12.36 C ATOM 1771 C THR A 228 −19.067 8.438 13.272 1.00 10.02 C ATOM 1772 O THR A 228 −19.946 7.580 13.400 1.00 10.20 O ATOM 1773 CB THR A 228 −17.994 8.324 15.523 1.00 15.46 C ATOM 1774 OG1 THR A 228 −18.544 9.596 15.893 1.00 17.33 O ATOM 1775 CG2 THR A 228 −16.710 8.077 16.300 1.00 16.53 C ATOM 1776 N VAL A 229 −19.231 9.526 12.518 1.00 10.47 N ATOM 1777 CA VAL A 229 −20.485 9.808 11.826 1.00 9.15 C ATOM 1778 C VAL A 229 −20.779 8.746 10.744 1.00 7.39 C ATOM 1779 O VAL A 229 −19.859 8.294 10.059 1.00 8.94 O ATOM 1780 CB VAL A 229 −20.438 11.233 11.185 1.00 11.08 C ATOM 1781 CG1 VAL A 229 −19.367 11.300 10.106 1.00 13.13 C ATOM 1782 CG2 VAL A 229 −21.788 11.640 10.626 1.00 12.72 C ATOM 1783 N PRO A 230 −22.041 8.320 10.620 1.00 7.45 N ATOM 1784 CA PRO A 230 −22.387 7.423 9.507 1.00 6.36 C ATOM 1785 C PRO A 230 −22.051 8.070 8.168 1.00 9.18 C ATOM 1786 O PRO A 230 −22.254 9.273 8.002 1.00 10.77 O ATOM 1787 CB PRO A 230 −23.898 7.272 9.630 1.00 9.15 C ATOM 1788 CG PRO A 230 −24.173 7.499 11.112 1.00 9.93 C ATOM 1789 CD PRO A 230 −23.181 8.547 11.527 1.00 10.30 C ATOM 1790 N PHE A 231 −21.543 7.296 7.211 1.00 6.79 N ATOM 1791 CA PHE A 231 −21.343 7.874 5.886 1.00 7.46 C ATOM 1792 C PHE A 231 −21.514 6.920 4.722 1.00 7.73 C ATOM 1793 O PHE A 231 −21.356 5.690 4.853 1.00 7.65 O ATOM 1794 CB PHE A 231 −20.019 8.643 5.779 1.00 7.69 C ATOM 1795 CG PHE A 231 −18.787 7.796 5.905 1.00 7.77 C ATOM 1796 CD1 PHE A 231 −18.230 7.177 4.784 1.00 9.21 C ATOM 1797 CD2 PHE A 231 −18.145 7.656 7.125 1.00 8.70 C ATOM 1798 CE1 PHE A 231 −17.076 6.414 4.892 1.00 10.86 C ATOM 1799 CE2 PHE A 231 −16.986 6.901 7.243 1.00 9.68 C ATOM 1800 CZ PHE A 231 −16.446 6.274 6.122 1.00 10.56 C ATOM 1801 N LEU A 232 −21.861 7.532 3.590 1.00 7.02 N ATOM 1802 CA LEU A 232 −21.907 6.871 2.291 1.00 5.67 C ATOM 1803 C LEU A 232 −20.836 7.551 1.462 1.00 7.56 C ATOM 1804 O LEU A 232 −20.824 8.788 1.349 1.00 8.41 O ATOM 1805 CB LEU A 232 −23.257 7.105 1.638 1.00 7.44 C ATOM 1806 CG LEU A 232 −23.360 6.631 0.181 1.00 8.89 C ATOM 1807 CD1 LEU A 232 −23.158 5.113 0.097 1.00 9.59 C ATOM 1808 CD2 LEU A 232 −24.689 7.035 −0.430 1.00 9.38 C ATOM 1809 N LEU A 233 −19.937 6.755 0.893 1.00 5.98 N ATOM 1810 CA LEU A 233 −18.816 7.251 0.123 1.00 5.46 C ATOM 1811 C LEU A 233 −18.961 6.736 −1.311 1.00 6.46 C ATOM 1812 O LEU A 233 −19.020 5.524 −1.546 1.00 8.99 O ATOM 1813 CB LEU A 233 −17.536 6.719 0.749 1.00 6.96 C ATOM 1814 CG LEU A 233 −16.204 6.995 0.085 1.00 11.73 C ATOM 1815 CD1 LEU A 233 −15.985 8.484 −0.098 1.00 11.86 C ATOM 1816 CD2 LEU A 233 −15.087 6.376 0.926 1.00 11.71 C ATOM 1817 N LEU A 234 −19.047 7.664 −2.266 1.00 6.30 N ATOM 1818 CA LEU A 234 −19.146 7.328 −3.690 1.00 5.53 C ATOM 1819 C LEU A 234 −17.887 7.806 −4.387 1.00 6.67 C ATOM 1820 O LEU A 234 −17.482 8.964 −4.214 1.00 7.50 O ATOM 1821 CB LEU A 234 −20.366 8.015 −4.299 1.00 7.09 C ATOM 1822 CG LEU A 234 −21.692 7.778 −3.587 1.00 7.45 C ATOM 1823 CD1 LEU A 234 −22.809 8.556 −4.278 1.00 12.21 C ATOM 1824 CD2 LEU A 234 −22.056 6.295 −3.498 1.00 10.51 C ATOM 1825 N GLN A 235 −17.263 6.930 −5.172 1.00 6.02 N ATOM 1826 CA GLN A 235 −15.962 7.230 −5.746 1.00 6.69 C ATOM 1827 C GLN A 235 −15.826 6.601 −7.122 1.00 7.26 C ATOM 1828 O GLN A 235 −16.188 5.433 −7.310 1.00 9.83 O ATOM 1829 CB GLN A 235 −14.878 6.664 −4.823 1.00 8.10 C ATOM 1830 CG GLN A 235 −13.460 6.805 −5.331 1.00 8.78 C ATOM 1831 CD GLN A 235 −12.945 8.235 −5.263 1.00 14.60 C ATOM 1832 OE1 GLN A 235 −13.229 8.969 −4.310 1.00 11.92 O ATOM 1833 NE2 GLN A 235 −12.176 8.639 −6.273 1.00 14.30 N ATOM 1834 N GLY A 236 −15.324 7.367 −8.092 1.00 7.16 N ATOM 1835 CA GLY A 236 −15.027 6.814 −9.410 1.00 7.05 C ATOM 1836 C GLY A 236 −13.626 6.241 −9.448 1.00 7.13 C ATOM 1837 O GLY A 236 −12.698 6.781 −8.847 1.00 9.31 O ATOM 1838 N SER A 237 −13.451 5.143 −10.182 1.00 7.90 N ATOM 1839 CA SER A 237 −12.139 4.515 −10.244 1.00 10.56 C ATOM 1840 C SER A 237 −11.158 5.288 −11.122 1.00 8.69 C ATOM 1841 O SER A 237 −9.947 5.107 −11.016 1.00 12.81 O ATOM 1842 CB SER A 237 −12.244 3.065 −10.734 1.00 14.27 C ATOM 1843 OG SER A 237 −12.468 3.007 −12.137 1.00 14.14 O ATOM 1844 N ALA A 238 −11.676 6.132 −12.009 1.00 8.64 N ATOM 1845 CA ALA A 238 −10.806 6.884 −12.918 1.00 12.93 C ATOM 1846 C ALA A 238 −10.783 8.358 −12.539 1.00 12.31 C ATOM 1847 O ALA A 238 −10.740 9.239 −13.402 1.00 11.93 O ATOM 1848 CB ALA A 238 −11.257 6.704 −14.359 1.00 11.58 C ATOM 1849 N ASP A 239 −10.803 8.616 −11.238 1.00 9.91 N ATOM 1850 CA ASP A 239 −10.753 9.975 −10.703 1.00 11.61 C ATOM 1851 C ASP A 239 −9.331 10.528 −10.745 1.00 11.01 C ATOM 1852 O ASP A 239 −8.434 10.018 −10.070 1.00 12.82 O ATOM 1853 CB ASP A 239 −11.255 9.950 −9.260 1.00 9.49 C ATOM 1854 CG ASP A 239 −11.495 11.338 −8.701 1.00 10.07 C ATOM 1855 OD1 ASP A 239 −10.756 12.276 −9.080 1.00 9.43 O ATOM 1856 OD2 ASP A 239 −12.430 11.490 −7.888 1.00 10.75 O ATOM 1857 N ARG A 240 −9.131 11.573 −11.549 1.00 10.38 N ATOM 1858 CA ARG A 240 −7.807 12.154 −11.748 1.00 11.86 C ATOM 1859 C ARG A 240 −7.387 13.173 −10.695 1.00 13.94 C ATOM 1860 O ARG A 240 −6.243 13.631 −10.692 1.00 15.63 O ATOM 1861 CB ARG A 240 −7.736 12.819 −13.124 1.00 15.76 C ATOM 1862 CG ARG A 240 −7.703 11.848 −14.277 1.00 26.43 C ATOM 1863 CD ARG A 240 −6.677 12.317 −15.281 1.00 32.76 C ATOM 1864 NE ARG A 240 −6.988 11.882 −16.633 1.00 71.10 N ATOM 1865 CZ ARG A 240 −6.466 12.441 −17.716 1.00 19.70 C ATOM 1866 NH1 ARG A 240 −5.618 13.457 −17.587 1.00 26.60 N ATOM 1867 NH2 ARG A 240 −6.798 11.989 −18.914 1.00 79.96 N ATOM 1868 N LEU A 241 −8.305 13.521 −9.803 1.00 10.36 N ATOM 1869 CA LEU A 241 −8.077 14.586 −8.841 1.00 12.06 C ATOM 1870 C LEU A 241 −8.030 14.068 −7.404 1.00 14.79 C ATOM 1871 O LEU A 241 −7.048 14.283 −6.685 1.00 17.27 O ATOM 1872 CB LEU A 241 −9.189 15.621 −8.995 1.00 12.48 C ATOM 1873 CG LEU A 241 −8.962 16.968 −8.329 1.00 17.56 C ATOM 1874 CD1 LEU A 241 −7.606 17.547 −8.721 1.00 17.75 C ATOM 1875 CD2 LEU A 241 −10.086 17.899 −8.744 1.00 14.80 C ATOM 1876 N CYS A 242 −9.103 13.402 −6.990 1.00 13.17 N ATOM 1877 CA CYS A 242 −9.172 12.777 −5.674 1.00 14.00 C ATOM 1878 C CYS A 242 −8.910 11.295 −5.861 1.00 12.30 C ATOM 1879 O CYS A 242 −9.775 10.554 −6.343 1.00 16.19 O ATOM 1880 CB CYS A 242 −10.531 13.035 −5.026 1.00 14.14 C ATOM 1881 SG CYS A 242 −10.791 14.786 −4.632 1.00 17.18 S ATOM 1882 N ASP A 243 −7.701 10.872 −5.514 1.00 14.74 N ATOM 1883 CA ASP A 243 −7.270 9.511 −5.787 1.00 15.90 C ATOM 1884 C ASP A 243 −8.125 8.489 −5.046 1.00 18.69 C ATOM 1885 O ASP A 243 −8.421 8.649 −3.860 1.00 14.40 O ATOM 1886 CB ASP A 243 −5.804 9.327 −5.418 1.00 17.66 C ATOM 1887 CG ASP A 243 −5.180 8.144 −6.122 1.00 49.96 C ATOM 1888 OD1 ASP A 243 −4.757 8.299 −7.289 1.00 39.78 O ATOM 1889 OD2 ASP A 243 −5.123 7.057 −5.512 1.00 25.88 O ATOM 1890 N SER A 244 −8.527 7.436 −5.748 1.00 15.66 N ATOM 1891 CA SER A 244 −9.378 6.416 −5.142 1.00 17.72 C ATOM 1892 C SER A 244 −8.736 5.808 −3.894 1.00 15.64 C ATOM 1893 O SER A 244 −9.435 5.302 −3.025 1.00 15.29 O ATOM 1894 CB SER A 244 −9.721 5.322 −6.155 1.00 17.74 C ATOM 1895 OG SER A 244 −8.542 4.671 −6.580 1.00 20.33 O ATOM 1896 N LYS A 245 −7.412 5.860 −3.800 1.00 14.32 N ATOM 1897 CA LYS A 245 −6.711 5.394 −2.606 1.00 12.72 C ATOM 1898 C LYS A 245 −7.198 6.097 −1.339 1.00 16.08 C ATOM 1899 O LYS A 245 −7.211 5.508 −0.255 1.00 15.31 O ATOM 1900 CB LYS A 245 −5.203 5.593 −2.754 1.00 18.83 C ATOM 1901 CG LYS A 245 −4.394 5.124 −1.557 1.00 44.09 C ATOM 1902 CD LYS A 245 −2.929 5.507 −1.692 1.00 75.26 C ATOM 1903 CE LYS A 245 −2.150 5.169 −0.430 1.00 60.92 C ATOM 1904 NZ LYS A 245 −0.732 5.618 −0.513 1.00 81.77 N ATOM 1905 N GLY A 246 −7.597 7.357 −1.475 1.00 12.05 N ATOM 1906 CA GLY A 246 −8.129 8.112 −0.354 1.00 11.97 C ATOM 1907 C GLY A 246 −9.462 7.569 0.115 1.00 12.09 C ATOM 1908 O GLY A 246 −9.752 7.562 1.312 1.00 11.82 O ATOM 1909 N ALA A 247 −10.288 7.118 −0.820 1.00 11.78 N ATOM 1910 CA ALA A 247 −11.562 6.515 −0.461 1.00 12.42 C ATOM 1911 C ALA A 247 −11.315 5.279 0.404 1.00 11.27 C ATOM 1912 O ALA A 247 −11.993 5.079 1.417 1.00 11.32 O ATOM 1913 CB ALA A 247 −12.369 6.151 −1.713 1.00 11.97 C ATOM 1914 N TYR A 248 −10.349 4.451 0.001 1.00 11.26 N ATOM 1915 CA TYR A 248 −10.022 3.256 0.776 1.00 12.36 C ATOM 1916 C TYR A 248 −9.458 3.631 2.155 1.00 12.09 C ATOM 1917 O TYR A 248 −9.752 2.971 3.152 1.00 11.59 O ATOM 1918 CB TYR A 248 −9.074 2.322 0.001 1.00 11.60 C ATOM 1919 CG TYR A 248 −9.652 1.861 −1.322 1.00 14.61 C ATOM 1920 CD1 TYR A 248 −10.872 1.201 −1.371 1.00 13.55 C ATOM 1921 CD2 TYR A 248 −8.985 2.092 −2.520 1.00 19.12 C ATOM 1922 CE1 TYR A 248 −11.419 0.784 −2.571 1.00 18.03 C ATOM 1923 CE2 TYR A 248 −9.528 1.677 −3.728 1.00 19.37 C ATOM 1924 CZ TYR A 248 −10.743 1.025 −3.742 1.00 16.03 C ATOM 1925 OH TYR A 248 −11.302 0.600 −4.929 1.00 19.87 O ATOM 1926 N LEU A 249 −8.673 4.703 2.215 1.00 11.41 N ATOM 1927 CA LEU A 249 −8.116 5.181 3.484 1.00 10.25 C ATOM 1928 C LEU A 249 −9.220 5.627 4.447 1.00 10.35 C ATOM 1929 O LEU A 249 −9.189 5.328 5.647 1.00 10.53 O ATOM 1930 CB LEU A 249 −7.150 6.339 3.226 1.00 13.46 C ATOM 1931 CG LEU A 249 −6.365 6.824 4.444 1.00 18.08 C ATOM 1932 CD1 LEU A 249 −5.351 5.760 4.858 1.00 19.06 C ATOM 1933 CD2 LEU A 249 −5.667 8.146 4.150 1.00 18.48 C ATOM 1934 N LEU A 250 −10.209 6.336 3.923 1.00 9.37 N ATOM 1935 CA LEU A 250 −11.329 6.757 4.724 1.00 9.21 C ATOM 1936 C LEU A 250 −12.080 5.543 5.271 1.00 12.66 C ATOM 1937 O LEU A 250 −12.435 5.510 6.450 1.00 11.83 O ATOM 1938 CB LEU A 250 −12.235 7.661 3.897 1.00 13.06 C ATOM 1939 CG LEU A 250 −13.559 8.092 4.496 1.00 13.37 C ATOM 1940 CD1 LEU A 250 −13.375 8.747 5.858 1.00 14.48 C ATOM 1941 CD2 LEU A 250 −14.209 9.066 3.529 1.00 16.04 C ATOM 1942 N MET A 251 −12.304 4.531 4.431 1.00 9.91 N ATOM 1943 CA MET A 251 −12.998 3.327 4.888 1.00 10.56 C ATOM 1944 C MET A 251 −12.189 2.596 5.950 1.00 10.04 C ATOM 1945 O MET A 251 −12.759 1.991 6.860 1.00 13.87 O ATOM 1946 CB MET A 251 −13.284 2.381 3.719 1.00 9.50 C ATOM 1947 CG MET A 251 −14.342 2.899 2.762 1.00 13.01 C ATOM 1948 SD MET A 251 −15.992 3.057 3.473 1.00 11.08 S ATOM 1949 CE MET A 251 −16.458 1.331 3.656 1.00 12.29 C ATOM 1950 N GLU A 252 −10.872 2.640 5.835 1.00 8.28 N ATOM 1951 CA GLU A 252 −10.013 1.916 6.763 1.00 10.79 C ATOM 1952 C GLU A 252 −9.890 2.619 8.110 1.00 14.17 C ATOM 1953 O GLU A 252 −9.960 1.979 9.162 1.00 16.34 O ATOM 1954 CB GLU A 252 −8.620 1.717 6.171 1.00 14.04 C ATOM 1955 CG GLU A 252 −7.682 0.962 7.109 1.00 18.86 C ATOM 1956 CD GLU A 252 −6.248 0.940 6.620 1.00 88.82 C ATOM 1957 OE1 GLU A 252 −5.970 1.541 5.561 1.00 68.03 O ATOM 1958 OE2 GLU A 252 −5.398 0.324 7.297 1.00 99.02 O ATOM 1959 N LEU A 253 −9.701 3.933 8.082 1.00 11.41 N ATOM 1960 CA LEU A 253 −9.336 4.662 9.294 1.00 11.04 C ATOM 1961 C LEU A 253 −10.506 5.218 10.100 1.00 11.58 C ATOM 1962 O LEU A 253 −10.383 5.395 11.309 1.00 14.92 O ATOM 1963 CB LEU A 253 −8.355 5.785 8.958 1.00 14.04 C ATOM 1964 CG LEU A 253 −6.961 5.350 8.512 1.00 15.41 C ATOM 1965 CD1 LEU A 253 −6.066 6.565 8.335 1.00 19.75 C ATOM 1966 CD2 LEU A 253 −6.354 4.367 9.504 1.00 26.28 C ATOM 1967 N ALA A 254 −11.625 5.526 9.451 1.00 9.74 N ATOM 1968 CA ALA A 254 −12.783 6.055 10.171 1.00 10.79 C ATOM 1969 C ALA A 254 −13.301 5.031 11.184 1.00 12.72 C ATOM 1970 O ALA A 254 −13.301 3.828 10.913 1.00 13.12 O ATOM 1971 CB ALA A 254 −13.887 6.452 9.198 1.00 13.02 C ATOM 1972 N LYS A 255 −13.738 5.502 12.347 1.00 11.30 N ATOM 1973 CA LYS A 255 −14.265 4.593 13.360 1.00 13.33 C ATOM 1974 C LYS A 255 −15.774 4.394 13.233 1.00 14.71 C ATOM 1975 O LYS A 255 −16.377 3.634 13.992 1.00 16.28 O ATOM 1976 CB LYS A 255 −13.899 5.072 14.772 1.00 17.14 C ATOM 1977 CG LYS A 255 −12.399 5.098 15.036 1.00 23.75 C ATOM 1978 CD LYS A 255 −11.776 3.721 14.861 1.00 30.83 C ATOM 1979 CE LYS A 255 −10.267 3.744 15.092 1.00 45.25 C ATOM 1980 NZ LYS A 255 −9.509 4.223 13.898 1.00 43.77 N ATOM 1981 N SER A 256 −16.387 5.067 12.265 1.00 10.29 N ATOM 1982 CA SER A 256 −17.821 4.987 12.074 1.00 9.83 C ATOM 1983 C SER A 256 −18.307 3.548 12.017 1.00 9.52 C ATOM 1984 O SER A 256 −17.734 2.720 11.306 1.00 12.49 O ATOM 1985 CB SER A 256 −18.221 5.704 10.779 1.00 11.18 C ATOM 1986 OG SER A 256 −17.631 6.993 10.743 1.00 11.20 O ATOM 1987 N GLN A 257 −19.374 3.264 12.747 1.00 9.12 N ATOM 1988 CA GLN A 257 −20.003 1.942 12.704 1.00 12.22 C ATOM 1989 C GLN A 257 −20.865 1.739 11.464 1.00 13.06 C ATOM 1990 O GLN A 257 −21.242 0.613 11.143 1.00 14.98 O ATOM 1991 CB GLN A 257 −20.847 1.714 13.959 1.00 13.19 C ATOM 1992 CG GLN A 257 −20.018 1.658 15.238 1.00 16.99 C ATOM 1993 CD GLN A 257 −20.834 1.258 16.450 1.00 67.11 C ATOM 1994 OE1 GLN A 257 −22.052 1.432 16.479 1.00 74.68 O ATOM 1995 NE2 GLN A 257 −20.163 0.719 17.462 1.00 83.33 N ATOM 1996 N ASP A 258 −21.186 2.829 10.772 1.00 8.32 N ATOM 1997 CA ASP A 258 −22.065 2.767 9.614 1.00 9.96 C ATOM 1998 C ASP A 258 −21.342 3.413 8.433 1.00 9.10 C ATOM 1999 O ASP A 258 −21.434 4.625 8.226 1.00 10.80 O ATOM 2000 CB ASP A 258 −23.365 3.512 9.942 1.00 8.32 C ATOM 2001 CG ASP A 258 −24.395 3.468 8.825 1.00 11.84 C ATOM 2002 OD1 ASP A 258 −24.184 2.773 7.806 1.00 11.26 O ATOM 2003 OD2 ASP A 258 −25.450 4.120 8.973 1.00 13.37 O ATOM 2004 N LYS A 259 −20.599 2.614 7.677 1.00 6.95 N ATOM 2005 CA LYS A 259 −19.839 3.150 6.547 1.00 7.68 C ATOM 2006 C LYS A 259 −19.924 2.230 5.339 1.00 9.90 C ATOM 2007 O LYS A 259 −19.757 1.001 5.443 1.00 10.58 O ATOM 2008 CB LYS A 259 −18.389 3.463 6.914 1.00 12.50 C ATOM 2009 CG LYS A 259 −17.667 2.376 7.675 1.00 10.44 C ATOM 2010 CD LYS A 259 −16.259 2.799 8.055 1.00 10.64 C ATOM 2011 CE LYS A 259 −15.610 1.749 8.959 1.00 11.27 C ATOM 2012 NZ LYS A 259 −14.164 1.975 9.132 1.00 11.78 N ATOM 2013 N THR A 260 −20.192 2.846 4.192 1.00 6.48 N ATOM 2014 CA ATHR A 260 −20.426 2.128 2.937 0.70 5.21 C ATOM 2015 C THR A 260 −19.679 2.820 1.804 1.00 7.56 C ATOM 2016 O THR A 260 −19.699 4.058 1.710 1.00 8.70 O ATOM 2017 CB ATHR A 260 −21.925 2.119 2.590 0.70 7.13 C ATOM 2018 OG1 ATHR A 260 −22.686 1.596 3.693 0.70 8.97 O ATOM 2019 CG2 ATHR A 260 −22.190 1.270 1.340 0.70 8.35 C ATOM 2020 CA BTHR A 260 −20.360 2.105 2.955 0.30 8.55 C ATOM 2021 CB BTHR A 260 −21.842 1.896 2.629 0.30 10.28 C ATOM 2022 OG1 BTHR A 260 −22.498 3.164 2.524 0.30 15.39 O ATOM 2023 CG2 BTHR A 260 −22.511 1.083 3.722 0.30 17.62 C ATOM 2024 N LEU A 261 −19.051 2.029 0.942 1.00 5.66 N ATOM 2025 CA LEU A 261 −18.343 2.540 −0.225 1.00 7.03 C ATOM 2026 C LEU A 261 −18.930 1.930 −1.486 1.00 8.11 C ATOM 2027 O LEU A 261 −19.079 0.710 −1.580 1.00 8.85 O ATOM 2028 CB LEU A 261 −16.878 2.162 −0.147 1.00 8.55 C ATOM 2029 CG LEU A 261 −16.055 2.355 −1.429 1.00 7.61 C ATOM 2030 CD1 LEU A 261 −15.940 3.844 −1.802 1.00 10.12 C ATOM 2031 CD2 LEU A 261 −14.679 1.753 −1.241 1.00 9.79 C ATOM 2032 N LYS A 262 −19.273 2.775 −2.459 1.00 5.57 N ATOM 2033 CA LYS A 262 −19.587 2.288 −3.810 1.00 7.37 C ATOM 2034 C LYS A 262 −18.569 2.856 −4.785 1.00 9.49 C ATOM 2035 O LYS A 262 −18.314 4.066 −4.798 1.00 9.23 O ATOM 2036 CB LYS A 262 −20.996 2.686 −4.224 1.00 9.44 C ATOM 2037 CG LYS A 262 −21.487 2.018 −5.527 1.00 14.01 C ATOM 2038 CD LYS A 262 −22.988 2.224 −5.735 1.00 17.20 C ATOM 2039 CE LYS A 262 −23.449 1.716 −7.104 1.00 18.72 C ATOM 2040 NZ LYS A 262 −23.405 0.223 −7.191 1.00 18.42 N ATOM 2041 N ILE A 263 −17.949 1.975 −5.567 1.00 7.42 N ATOM 2042 CA AILE A 263 −16.971 2.372 −6.583 0.90 9.22 C ATOM 2043 C ILE A 263 −17.617 2.289 −7.953 1.00 7.84 C ATOM 2044 O ILE A 263 −18.215 1.266 −8.303 1.00 9.35 O ATOM 2045 CB AILE A 263 −15.715 1.470 −6.574 0.90 9.09 C ATOM 2046 CG1 AILE A 263 −14.885 1.681 −5.301 0.90 11.72 C ATOM 2047 CG2 AILE A 263 −14.865 1.719 −7.834 0.90 11.99 C ATOM 2048 CD1 AILE A 263 −14.085 2.991 −5.280 0.90 11.94 C ATOM 2049 CA BILE A 263 −16.994 2.399 −6.575 0.10 10.98 C ATOM 2050 CB BILE A 263 −15.721 1.559 −6.521 0.10 6.66 C ATOM 2051 CG1 BILE A 263 −15.124 1.623 −5.119 0.10 7.98 C ATOM 2052 CG2 BILE A 263 −14.718 2.040 −7.561 0.10 17.27 C ATOM 2053 CD1 BILE A 263 −13.981 0.698 −4.927 0.10 3.99 C ATOM 2054 N TYR A 264 −17.498 3.363 −8.726 1.00 7.78 N ATOM 2055 CA TYR A 264 −18.012 3.401 −10.095 1.00 9.35 C ATOM 2056 C TYR A 264 −16.856 3.194 −11.063 1.00 8.73 C ATOM 2057 O TYR A 264 −16.002 4.063 −11.239 1.00 7.97 O ATOM 2058 CB TYR A 264 −18.727 4.723 −10.348 1.00 9.49 C ATOM 2059 CG TYR A 264 −20.043 4.815 −9.615 1.00 5.92 C ATOM 2060 CD1 TYR A 264 −21.221 4.371 −10.195 1.00 9.53 C ATOM 2061 CD2 TYR A 264 −20.108 5.343 −8.330 1.00 10.30 C ATOM 2062 CE1 TYR A 264 −22.440 4.448 −9.525 1.00 10.75 C ATOM 2063 CE2 TYR A 264 −21.316 5.425 −7.650 1.00 8.15 C ATOM 2064 CZ TYR A 264 −22.476 4.978 −8.241 1.00 8.75 C ATOM 2065 OH TYR A 264 −23.684 5.059 −7.585 1.00 10.60 O ATOM 2066 N GLU A 265 −16.811 2.008 −11.667 1.00 9.58 N ATOM 2067 CA GLU A 265 −15.690 1.611 −12.504 1.00 12.10 C ATOM 2068 C GLU A 265 −15.638 2.432 −13.796 1.00 8.46 C ATOM 2069 O GLU A 265 −16.606 2.477 −14.549 1.00 11.89 O ATOM 2070 CB GLU A 265 −15.789 0.114 −12.824 1.00 16.13 C ATOM 2071 CG GLU A 265 −14.547 −0.464 −13.462 1.00 17.85 C ATOM 2072 CD GLU A 265 −13.347 −0.469 −12.534 1.00 21.43 C ATOM 2073 OE1 GLU A 265 −13.508 −0.218 −11.312 1.00 20.61 O ATOM 2074 OE2 GLU A 265 −12.227 −0.726 −13.020 1.00 32.40 O ATOM 2075 N GLY A 266 −14.507 3.096 −14.005 1.00 9.44 N ATOM 2076 CA GLY A 266 −14.289 3.887 −15.205 1.00 11.21 C ATOM 2077 C GLY A 266 −14.797 5.313 −15.075 1.00 11.31 C ATOM 2078 O GLY A 266 −14.514 6.145 −15.936 1.00 10.95 O ATOM 2079 N ALA A 267 −15.548 5.598 −14.015 1.00 9.68 N ATOM 2080 CA ALA A 267 −16.150 6.920 −13.851 1.00 10.27 C ATOM 2081 C ALA A 267 −15.114 7.942 −13.397 1.00 6.06 C ATOM 2082 O ALA A 267 −14.166 7.627 −12.691 1.00 7.71 O ATOM 2083 CB ALA A 267 −17.324 6.859 −12.875 1.00 9.22 C ATOM 2084 N TYR A 268 −15.291 9.176 −13.865 1.00 7.32 N ATOM 2085 CA TYR A 268 −14.391 10.267 −13.504 1.00 7.50 C ATOM 2086 C TYR A 268 −14.858 10.929 −12.194 1.00 9.01 C ATOM 2087 O TYR A 268 −15.804 10.481 −11.556 1.00 11.16 O ATOM 2088 CB TYR A 268 −14.357 11.317 −14.632 1.00 8.84 C ATOM 2089 CG TYR A 268 −13.629 10.892 −15.905 1.00 9.04 C ATOM 2090 CD1 TYR A 268 −13.218 9.575 −16.106 1.00 12.36 C ATOM 2091 CD2 TYR A 268 −13.385 11.812 −16.915 1.00 10.68 C ATOM 2092 CE1 TYR A 268 −12.557 9.193 −17.278 1.00 13.18 C ATOM 2093 CE2 TYR A 268 −12.736 11.442 −18.087 1.00 15.29 C ATOM 2094 CZ TYR A 268 −12.324 10.140 −18.259 1.00 14.67 C ATOM 2095 OH TYR A 268 −11.687 9.783 −19.436 1.00 17.75 O ATOM 2096 N HIS A 269 −14.191 12.013 −11.834 1.00 7.57 N ATOM 2097 CA HIS A 269 −14.368 12.696 −10.548 1.00 6.36 C ATOM 2098 C HIS A 269 −15.795 13.154 −10.224 1.00 7.22 C ATOM 2099 O HIS A 269 −16.295 12.928 −9.115 1.00 7.15 O ATOM 2100 CB HIS A 269 −13.421 13.898 −10.549 1.00 7.11 C ATOM 2101 CG HIS A 269 −13.401 14.689 −9.274 1.00 7.54 C ATOM 2102 ND1 HIS A 269 −13.058 14.144 −8.053 1.00 9.09 N ATOM 2103 CD2 HIS A 269 −13.599 16.012 −9.051 1.00 9.50 C ATOM 2104 CE1 HIS A 269 −13.070 15.096 −7.130 1.00 8.18 C ATOM 2105 NE2 HIS A 269 −13.393 16.237 −7.711 1.00 10.12 N ATOM 2106 N VAL A 270 −16.464 13.813 −11.161 1.00 6.45 N ATOM 2107 CA VAL A 270 −17.721 14.471 −10.832 1.00 6.65 C ATOM 2108 C VAL A 270 −18.897 13.531 −11.071 1.00 7.38 C ATOM 2109 O VAL A 270 −19.610 13.613 −12.081 1.00 6.78 O ATOM 2110 CB VAL A 270 −17.896 15.798 −11.602 1.00 5.79 C ATOM 2111 CG1 VAL A 270 −19.038 16.584 −10.997 1.00 7.82 C ATOM 2112 CG2 VAL A 270 −16.630 16.622 −11.516 1.00 7.71 C ATOM 2113 N LEU A 271 −19.103 12.637 −10.108 1.00 6.65 N ATOM 2114 CA LEU A 271 −20.053 11.534 −10.285 1.00 6.15 C ATOM 2115 C LEU A 271 −21.499 11.970 −10.477 1.00 5.91 C ATOM 2116 O LEU A 271 −22.285 11.283 −11.133 1.00 7.39 O ATOM 2117 CB LEU A 271 −19.957 10.556 −9.105 1.00 6.48 C ATOM 2118 CG LEU A 271 −18.615 9.871 −8.906 1.00 5.62 C ATOM 2119 CD1 LEU A 271 −18.659 9.055 −7.613 1.00 9.62 C ATOM 2120 CD2 LEU A 271 −18.321 8.957 −10.089 1.00 8.14 C ATOM 2121 N HIS A 272 −21.873 13.103 −9.886 1.00 5.74 N ATOM 2122 CA HIS A 272 −23.233 13.610 −10.006 1.00 5.90 C ATOM 2123 C HIS A 272 −23.448 14.420 −11.291 1.00 5.61 C ATOM 2124 O HIS A 272 −24.538 14.940 −11.511 1.00 8.27 O ATOM 2125 CB HIS A 272 −23.602 14.449 −8.773 1.00 6.29 C ATOM 2126 CG HIS A 272 −22.612 15.529 −8.463 1.00 8.33 C ATOM 2127 ND1 HIS A 272 −21.309 15.262 −8.108 1.00 8.50 N ATOM 2128 CD2 HIS A 272 −22.731 16.879 −8.481 1.00 11.04 C ATOM 2129 CE1 HIS A 272 −20.669 16.402 −7.905 1.00 12.80 C ATOM 2130 NE2 HIS A 272 −21.510 17.396 −8.128 1.00 11.63 N ATOM 2131 N LYS A 273 −22.403 14.505 −12.121 1.00 6.91 N ATOM 2132 CA LYS A 273 −22.487 15.162 −13.432 1.00 7.10 C ATOM 2133 C LYS A 273 −21.801 14.293 −14.470 1.00 7.81 C ATOM 2134 O LYS A 273 −21.114 14.800 −15.363 1.00 8.13 O ATOM 2135 CB LYS A 273 −21.778 16.519 −13.399 1.00 8.99 C ATOM 2136 CG LYS A 273 −22.307 17.505 −12.362 1.00 9.49 C ATOM 2137 CD LYS A 273 −23.666 18.011 −12.739 1.00 9.39 C ATOM 2138 CE LYS A 273 −24.085 19.150 −11.798 1.00 11.48 C ATOM 2139 NZ LYS A 273 −25.494 19.505 −12.017 1.00 16.06 N ATOM 2140 N GLU A 274 −21.948 12.978 −14.319 1.00 7.75 N ATOM 2141 CA GLU A 274 −21.254 12.023 −15.169 1.00 7.79 C ATOM 2142 C GLU A 274 −22.186 11.460 −16.249 1.00 7.03 C ATOM 2143 O GLU A 274 −23.236 12.024 −16.542 1.00 9.33 O ATOM 2144 CB GLU A 274 −20.654 10.908 −14.297 1.00 10.21 C ATOM 2145 CG GLU A 274 −19.145 10.870 −14.300 1.00 9.08 C ATOM 2146 CD GLU A 274 −18.598 10.004 −15.429 1.00 8.56 C ATOM 2147 OE1 GLU A 274 −17.403 10.118 −15.749 1.00 10.56 O ATOM 2148 OE2 GLU A 274 −19.388 9.210 −15.979 1.00 11.18 O ATOM 2149 N LEU A 275 −21.787 10.352 −16.869 1.00 8.50 N ATOM 2150 CA LEU A 275 −22.669 9.703 −17.836 1.00 9.61 C ATOM 2151 C LEU A 275 −23.985 9.365 −17.146 1.00 11.58 C ATOM 2152 O LEU A 275 −23.991 9.062 −15.954 1.00 10.17 O ATOM 2153 CB LEU A 275 −22.016 8.439 −18.394 1.00 9.97 C ATOM 2154 CG LEU A 275 −20.737 8.703 −19.181 1.00 12.18 C ATOM 2155 CD1 LEU A 275 −20.108 7.415 −19.713 1.00 14.42 C ATOM 2156 CD2 LEU A 275 −21.026 9.667 −20.329 1.00 15.54 C ATOM 2157 N PRO A 276 −25.107 9.413 −17.881 1.00 11.73 N ATOM 2158 CA PRO A 276 −26.427 9.164 −17.288 1.00 14.10 C ATOM 2159 C PRO A 276 −26.511 7.906 −16.417 1.00 16.89 C ATOM 2160 O PRO A 276 −27.109 7.964 −15.336 1.00 17.36 O ATOM 2161 CB PRO A 276 −27.334 9.016 −18.512 1.00 16.90 C ATOM 2162 CG PRO A 276 −26.692 9.878 −19.538 1.00 21.28 C ATOM 2163 CD PRO A 276 −25.205 9.809 −19.300 1.00 13.96 C ATOM 2164 N GLU A 277 −25.939 6.792 −16.870 1.00 14.89 N ATOM 2165 CA GLU A 277 −25.994 5.547 −16.100 1.00 16.63 C ATOM 2166 C GLU A 277 −25.385 5.732 −14.712 1.00 16.38 C ATOM 2167 O GLU A 277 −25.934 5.261 −13.712 1.00 19.95 O ATOM 2168 CB GLU A 277 −25.286 4.408 −16.841 1.00 21.94 C ATOM 2169 CG GLU A 277 −26.111 3.796 −17.961 1.00 85.26 C ATOM 2170 CD GLU A 277 −25.461 2.565 −18.564 1.00 121.84 C ATOM 2171 OE1 GLU A 277 −24.359 2.187 −18.112 1.00 109.89 O ATOM 2172 OE2 GLU A 277 −26.055 1.973 −19.490 1.00 104.17 O ATOM 2173 N VAL A 278 −24.252 6.421 −14.655 1.00 10.73 N ATOM 2174 CA VAL A 278 −23.595 6.693 −13.384 1.00 9.85 C ATOM 2175 C VAL A 278 −24.407 7.674 −12.541 1.00 11.95 C ATOM 2176 O VAL A 278 −24.734 7.391 −11.387 1.00 11.20 O ATOM 2177 CB VAL A 278 −22.169 7.242 −13.601 1.00 9.03 C ATOM 2178 CG1 VAL A 278 −21.597 7.780 −12.299 1.00 12.15 C ATOM 2179 CG2 VAL A 278 −21.269 6.158 −14.196 1.00 13.85 C ATOM 2180 N THR A 279 −24.757 8.814 −13.119 1.00 9.26 N ATOM 2181 CA THR A 279 −25.478 9.838 −12.372 1.00 10.05 C ATOM 2182 C THR A 279 −26.818 9.334 −11.848 1.00 9.97 C ATOM 2183 O THR A 279 −27.201 9.644 −10.721 1.00 10.35 O ATOM 2184 CB THR A 279 −25.640 11.119 −13.200 1.00 10.89 C ATOM 2185 OG1 THR A 279 −24.336 11.655 −13.456 1.00 15.41 O ATOM 2186 CG2 THR A 279 −26.464 12.144 −12.443 1.00 11.76 C ATOM 2187 N ASN A 280 −27.534 8.562 −12.660 1.00 10.65 N ATOM 2188 CA ASN A 280 −28.815 8.023 −12.224 1.00 11.97 C ATOM 2189 C ASN A 280 −28.632 7.108 −11.016 1.00 9.96 C ATOM 2190 O ASN A 280 −29.428 7.140 −10.067 1.00 10.76 O ATOM 2191 CB ASN A 280 −29.510 7.269 −13.360 1.00 11.47 C ATOM 2192 CG ASN A 280 −30.038 8.195 −14.441 1.00 21.55 C ATOM 2193 OD1 ASN A 280 −30.206 9.391 −14.221 1.00 21.86 O ATOM 2194 ND2 ASN A 280 −30.305 7.639 −15.617 1.00 25.48 N ATOM 2195 N SER A 281 −27.577 6.303 −11.056 1.00 9.62 N ATOM 2196 CA SER A 281 −27.240 5.423 −9.943 1.00 9.05 C ATOM 2197 C SER A 281 −26.862 6.227 −8.703 1.00 10.69 C ATOM 2198 O SER A 281 −27.311 5.922 −7.607 1.00 10.10 O ATOM 2199 CB SER A 281 −26.089 4.494 −10.331 1.00 9.22 C ATOM 2200 OG SER A 281 −25.601 3.798 −9.193 1.00 11.41 O ATOM 2201 N VAL A 282 −26.029 7.250 −8.878 1.00 8.01 N ATOM 2202 CA VAL A 282 −25.625 8.113 −7.769 1.00 9.36 C ATOM 2203 C VAL A 282 −26.851 8.703 −7.059 1.00 8.59 C ATOM 2204 O VAL A 282 −26.955 8.650 −5.827 1.00 8.36 O ATOM 2205 CB VAL A 282 −24.668 9.223 −8.262 1.00 8.18 C ATOM 2206 CG1 VAL A 282 −24.550 10.343 −7.228 1.00 8.83 C ATOM 2207 CG2 VAL A 282 −23.313 8.620 −8.597 1.00 9.21 C ATOM 2208 N PHE A 283 −27.787 9.254 −7.828 1.00 7.90 N ATOM 2209 CA PHE A 283 −29.005 9.804 −7.247 1.00 7.68 C ATOM 2210 C PHE A 283 −29.799 8.730 −6.507 1.00 10.02 C ATOM 2211 O PHE A 283 −30.290 8.961 −5.403 1.00 10.89 O ATOM 2212 CB PHE A 283 −29.881 10.463 −8.316 1.00 8.60 C ATOM 2213 CG PHE A 283 −29.534 11.907 −8.593 1.00 8.21 C ATOM 2214 CD1 PHE A 283 −28.295 12.257 −9.084 1.00 9.31 C ATOM 2215 CD2 PHE A 283 −30.478 12.907 −8.395 1.00 9.23 C ATOM 2216 CE1 PHE A 283 −27.977 13.595 −9.350 1.00 10.77 C ATOM 2217 CE2 PHE A 283 −30.172 14.238 −8.666 1.00 10.37 C ATOM 2218 CZ PHE A 283 −28.929 14.575 −9.137 1.00 10.84 C ATOM 2219 N HIS A 284 −29.932 7.556 −7.121 1.00 9.09 N ATOM 2220 CA HIS A 284 −30.675 6.463 −6.508 1.00 9.12 C ATOM 2221 C HIS A 284 −30.033 6.025 −5.189 1.00 9.99 C ATOM 2222 O HIS A 284 −30.737 5.828 −4.188 1.00 9.74 O ATOM 2223 CB HIS A 284 −30.765 5.290 −7.492 1.00 11.67 C ATOM 2224 CG HIS A 284 −31.431 4.069 −6.935 1.00 14.61 C ATOM 2225 ND1 HIS A 284 −32.760 4.046 −6.573 1.00 20.82 N ATOM 2226 CD2 HIS A 284 −30.958 2.820 −6.717 1.00 21.94 C ATOM 2227 CE1 HIS A 284 −33.074 2.837 −6.138 1.00 19.80 C ATOM 2228 NE2 HIS A 284 −31.998 2.075 −6.216 1.00 23.11 N ATOM 2229 N GLU A 285 −28.713 5.876 −5.181 1.00 8.55 N ATOM 2230 CA GLU A 285 −28.016 5.410 −3.977 1.00 8.60 C ATOM 2231 C GLU A 285 −28.134 6.419 −2.836 1.00 9.27 C ATOM 2232 O GLU A 285 −28.337 6.043 −1.678 1.00 10.15 O ATOM 2233 CB GLU A 285 −26.548 5.102 −4.266 1.00 10.27 C ATOM 2234 CG GLU A 285 −26.341 3.975 −5.284 1.00 12.66 C ATOM 2235 CD GLU A 285 −26.784 2.615 −4.761 1.00 48.46 C ATOM 2236 OE1 GLU A 285 −26.861 2.438 −3.526 1.00 24.33 O ATOM 2237 OE2 GLU A 285 −27.051 1.714 −5.586 1.00 26.17 O ATOM 2238 N ILE A 286 −27.999 7.703 −3.158 1.00 8.06 N ATOM 2239 CA ILE A 286 −28.130 8.738 −2.137 1.00 7.60 C ATOM 2240 C ILE A 286 −29.561 8.758 −1.615 1.00 8.03 C ATOM 2241 O ILE A 286 −29.797 8.844 −0.404 1.00 9.29 O ATOM 2242 CB ILE A 286 −27.726 10.117 −2.697 1.00 7.44 C ATOM 2243 CG1 ILE A 286 −26.225 10.131 −2.982 1.00 8.11 C ATOM 2244 CG2 ILE A 286 −28.104 11.222 −1.702 1.00 9.25 C ATOM 2245 CD1 ILE A 286 −25.730 11.355 −3.736 1.00 8.46 C ATOM 2246 N ASN A 287 −30.525 8.668 −2.524 1.00 7.56 N ATOM 2247 CA ASN A 287 −31.927 8.632 −2.145 1.00 9.10 C ATOM 2248 C ASN A 287 −32.196 7.506 −1.135 1.00 9.78 C ATOM 2249 O ASN A 287 −32.777 7.731 −0.068 1.00 10.92 O ATOM 2250 CB ASN A 287 −32.792 8.481 −3.408 1.00 9.77 C ATOM 2251 CG ASN A 287 −34.280 8.468 −3.121 1.00 16.23 C ATOM 2252 OD1 ASN A 287 −34.738 7.846 −2.167 1.00 16.90 O ATOM 2253 ND2 ASN A 287 −35.046 9.144 −3.968 1.00 17.83 N ATOM 2254 N MET A 288 −31.756 6.295 −1.457 1.00 9.68 N ATOM 2255 CA AMET A 288 −32.008 5.164 −0.571 0.75 10.52 C ATOM 2256 C MET A 288 −31.283 5.304 0.765 1.00 10.26 C ATOM 2257 O MET A 288 −31.858 5.002 1.817 1.00 11.11 O ATOM 2258 CB AMET A 288 −31.618 3.853 −1.246 0.75 13.43 C ATOM 2259 CG AMET A 288 −32.543 3.452 −2.384 0.75 11.44 C ATOM 2260 SD AMET A 288 −32.159 1.788 −2.967 0.75 19.23 S ATOM 2261 CE AMET A 288 −30.435 1.981 −3.415 0.75 25.05 C ATOM 2262 CA BMET A 288 −31.970 5.141 −0.586 0.25 13.65 C ATOM 2263 CB BMET A 288 −31.454 3.872 −1.264 0.25 10.56 C ATOM 2264 CG BMET A 288 −32.177 3.528 −2.550 0.25 11.01 C ATOM 2265 SD BMET A 288 −33.911 3.126 −2.263 0.25 15.84 S ATOM 2266 CE BMET A 288 −33.757 1.686 −1.209 0.25 35.78 C ATOM 2267 N TRP A 289 −30.041 5.768 0.732 1.00 8.12 N ATOM 2268 CA TRP A 289 −29.239 5.874 1.947 1.00 8.46 C ATOM 2269 C TRP A 289 −29.847 6.893 2.916 1.00 10.60 C ATOM 2270 O TRP A 289 −30.013 6.619 4.106 1.00 10.10 O ATOM 2271 CB TRP A 289 −27.809 6.262 1.588 1.00 8.04 C ATOM 2272 CG TRP A 289 −26.829 6.080 2.699 1.00 8.76 C ATOM 2273 CD1 TRP A 289 −26.110 4.953 2.987 1.00 8.96 C ATOM 2274 CD2 TRP A 289 −26.452 7.057 3.681 1.00 7.64 C ATOM 2275 NE1 TRP A 289 −25.307 5.171 4.076 1.00 8.96 N ATOM 2276 CE2 TRP A 289 −25.501 6.452 4.525 1.00 7.40 C ATOM 2277 CE3 TRP A 289 −26.815 8.386 3.916 1.00 8.72 C ATOM 2278 CZ2 TRP A 289 −24.912 7.130 5.594 1.00 8.56 C ATOM 2279 CZ3 TRP A 289 −26.232 9.055 4.981 1.00 9.78 C ATOM 2280 CH2 TRP A 289 −25.292 8.429 5.801 1.00 7.77 C ATOM 2281 N VAL A 290 −30.202 8.061 2.392 1.00 7.61 N ATOM 2282 CA VAL A 290 −30.822 9.098 3.210 1.00 8.87 C ATOM 2283 C VAL A 290 −32.228 8.697 3.658 1.00 11.01 C ATOM 2284 O VAL A 290 −32.591 8.898 4.821 1.00 12.42 O ATOM 2285 CB VAL A 290 −30.834 10.451 2.465 1.00 10.20 C ATOM 2286 CG1 VAL A 290 −31.622 11.483 3.254 1.00 13.69 C ATOM 2287 CG2 VAL A 290 −29.410 10.923 2.232 1.00 10.54 C ATOM 2288 N SER A 291 −33.018 8.122 2.757 1.00 11.05 N ATOM 2289 CA SER A 291 −34.362 7.653 3.105 1.00 12.68 C ATOM 2290 C SER A 291 −34.337 6.683 4.286 1.00 15.97 C ATOM 2291 O SER A 291 −35.128 6.805 5.226 1.00 16.56 O ATOM 2292 CB SER A 291 −35.013 6.968 1.903 1.00 14.10 C ATOM 2293 OG SER A 291 −35.461 7.922 0.957 1.00 20.61 O ATOM 2294 N GLN A 292 −33.428 5.717 4.236 1.00 13.80 N ATOM 2295 CA GLN A 292 −33.346 4.702 5.281 1.00 13.65 C ATOM 2296 C GLN A 292 −32.926 5.283 6.628 1.00 15.92 C ATOM 2297 O GLN A 292 −33.192 4.697 7.676 1.00 19.93 O ATOM 2298 CB GLN A 292 −32.414 3.577 4.841 1.00 15.28 C ATOM 2299 CG GLN A 292 −33.016 2.750 3.714 1.00 31.36 C ATOM 2300 CD GLN A 292 −32.018 1.827 3.059 1.00 59.35 C ATOM 2301 OE1 GLN A 292 −31.042 1.409 3.679 1.00 46.54 O ATOM 2302 NE2 GLN A 292 −32.259 1.500 1.795 1.00 52.18 N ATOM 2303 N ARG A 293 −32.290 6.449 6.604 1.00 11.83 N ATOM 2304 CA ARG A 293 −31.758 7.049 7.818 1.00 11.03 C ATOM 2305 C ARG A 293 −32.577 8.254 8.293 1.00 10.89 C ATOM 2306 O ARG A 293 −32.172 8.968 9.215 1.00 14.96 O ATOM 2307 CB ARG A 293 −30.273 7.380 7.632 1.00 9.52 C ATOM 2308 CG ARG A 293 −29.406 6.126 7.665 1.00 10.01 C ATOM 2309 CD ARG A 293 −28.042 6.325 7.036 1.00 10.98 C ATOM 2310 NE ARG A 293 −27.297 5.065 7.004 1.00 9.60 N ATOM 2311 CZ ARG A 293 −27.508 4.099 6.111 1.00 9.62 C ATOM 2312 NH1 ARG A 293 −28.431 4.249 5.166 1.00 9.87 N ATOM 2313 NH2 ARG A 293 −26.789 2.987 6.171 1.00 11.78 N ATOM 2314 N THR A 294 −33.731 8.453 7.667 1.00 14.09 N ATOM 2315 CA THR A 294 −34.681 9.485 8.068 1.00 15.85 C ATOM 2316 C THR A 294 −36.072 8.869 8.199 1.00 22.42 C ATOM 2317 O THR A 294 −37.067 9.584 8.311 1.00 36.87 O ATOM 2318 CB THR A 294 −34.731 10.651 7.053 1.00 16.73 C ATOM 2319 OG1 THR A 294 −35.000 10.137 5.743 1.00 18.85 O ATOM 2320 CG2 THR A 294 −33.417 11.393 7.022 1.00 15.10 C ATOM 2321 O01 INH I 1 −12.895 20.823 −4.999 1.00 7.09 O ATOM 2322 C02 INH I 1 −12.391 20.703 −6.129 1.00 8.09 C ATOM 2323 C03 INH I 1 −10.917 20.735 −6.329 1.00 7.66 C ATOM 2324 C04 INH I 1 −10.371 21.511 −7.372 1.00 8.80 C ATOM 2325 C05 INH I 1 −9.002 21.548 −7.621 1.00 11.29 C ATOM 2326 C06 INH I 1 −8.161 20.785 −6.808 1.00 9.74 C ATOM 2327 N07 INH I 1 −6.763 20.578 −6.783 1.00 12.42 N ATOM 2328 C08 INH I 1 −6.533 19.727 −5.790 1.00 14.65 C ATOM 2329 O09 INH I 1 −7.712 19.334 −5.112 1.00 13.07 O ATOM 2330 C10 INH I 1 −8.755 19.997 −5.760 1.00 9.91 C ATOM 2331 C11 INH I 1 −10.110 19.953 −5.499 1.00 7.61 C ATOM 2332 C12 INH I 1 −5.241 19.125 −5.317 1.00 16.69 C ATOM 2333 C13 INH I 1 −4.117 19.335 −6.328 1.00 15.09 C ATOM 2334 C14 INH I 1 −2.767 18.863 −5.823 1.00 19.81 C ATOM 2335 C15 INH I 1 −2.421 19.447 −4.476 1.00 19.20 C ATOM 2336 C16 INH I 1 −3.512 19.142 −3.467 1.00 19.60 C ATOM 2337 C17 INH I 1 −4.893 19.592 −3.914 1.00 17.98 C ATOM 2338 N18 INH I 1 −13.235 20.690 −7.197 1.00 6.87 N ATOM 2339 C19 INH I 1 −14.672 20.540 −7.283 1.00 6.93 C ATOM 2340 C20 INH I 1 −14.471 19.893 −8.684 1.00 6.67 C ATOM 2341 C21 INH I 1 −12.952 20.266 −8.587 1.00 8.77 C ATOM 2342 N22 INH I 1 −15.178 20.424 −9.813 1.00 6.45 N ATOM 2343 C23 INH I 1 −16.588 20.190 −9.789 1.00 5.98 C ATOM 2344 C24 INH I 1 −17.328 20.733 −11.042 1.00 6.80 C ATOM 2345 N25 INH I 1 −16.634 20.331 −12.248 1.00 7.33 N ATOM 2346 C26 INH I 1 −15.203 20.541 −12.284 1.00 10.22 C ATOM 2347 C27 INH I 1 −14.523 19.973 −11.038 1.00 7.33 C ATOM 2348 C28 INH I 1 −17.296 19.725 −13.318 1.00 6.80 C ATOM 2349 N29 INH I 1 −16.488 19.205 −14.329 1.00 7.30 N ATOM 2350 C30 INH I 1 −17.138 18.618 −15.336 1.00 7.90 C ATOM 2351 C31 INH I 1 −18.527 18.508 −15.408 1.00 7.42 C ATOM 2352 C32 INH I 1 −19.257 19.048 −14.354 1.00 7.83 C ATOM 2353 N33 INH I 1 −18.670 19.648 −13.307 1.00 6.45 N HETATM 2354 O HOH W 1 −17.954 27.691 4.082 1.00 7.52 O HETATM 2355 O HOH W 2 −16.687 30.118 3.647 1.00 7.58 O HETATM 2356 O HOH W 3 −16.903 29.964 −7.861 1.00 8.56 O HETATM 2357 O HOH W 4 −24.521 30.541 −6.460 1.00 8.76 O HETATM 2358 O HOH W 5 −18.264 32.412 10.389 1.00 8.02 O HETATM 2359 O HOH W 6 −23.247 3.675 5.398 1.00 9.13 O HETATM 2360 O HOH W 7 −15.105 23.282 −9.818 1.00 10.08 O HETATM 2361 O HOH W 8 −20.744 0.215 −8.443 1.00 9.73 O HETATM 2362 O HOH W 9 −11.897 30.578 −1.691 1.00 10.64 O HETATM 2363 O HOH W 10 −22.252 20.341 −15.373 1.00 11.45 O HETATM 2364 O HOH W 11 −27.187 18.469 −8.872 1.00 12.11 O HETATM 2365 O HOH W 12 −11.733 34.673 −0.588 1.00 12.31 O HETATM 2366 O HOH W 13 −11.423 12.123 −13.304 1.00 11.25 O HETATM 2367 O HOH W 14 −18.816 28.913 13.424 1.00 11.56 O HETATM 2368 O HOH W 15 −9.196 10.830 −2.094 1.00 12.11 O HETATM 2369 O HOH W 16 −9.803 26.896 −12.434 1.00 12.21 O HETATM 2370 O HOH W 17 −21.490 5.488 12.067 1.00 12.81 O HETATM 2371 O HOH W 18 −32.761 29.987 −2.012 1.00 14.02 O HETATM 2372 O HOH W 19 −18.414 31.657 13.060 1.00 12.16 O HETATM 2373 O HOH W 20 −5.462 30.956 −0.225 1.00 13.69 O HETATM 2374 O HOH W 21 −11.248 35.923 1.786 1.00 14.53 O HETATM 2375 O HOH W 22 −30.857 31.479 −3.105 1.00 12.95 O HETATM 2376 O HOH W 23 −17.537 30.497 −17.209 1.00 13.52 O HETATM 2377 O HOH W 24 −27.943 15.491 13.891 1.00 15.19 O HETATM 2378 O HOH W 25 −6.754 29.942 −6.600 1.00 14.74 O HETATM 2379 O HOH W 26 −21.995 24.699 −0.661 1.00 15.81 O HETATM 2380 O HOH W 27 −24.620 37.557 −8.143 1.00 14.70 O HETATM 2381 O HOH W 28 −11.836 10.105 −2.131 1.00 13.84 O HETATM 2382 O HOH W 29 −6.977 17.152 −20.873 1.00 14.48 O HETATM 2383 O HOH W 30 −27.778 25.779 17.062 1.00 14.55 O HETATM 2384 O HOH W 31 −28.099 20.389 −10.972 1.00 15.25 O HETATM 2385 O HOH W 32 −26.572 16.678 −10.935 1.00 15.41 O HETATM 2386 O HOH W 33 −21.236 20.183 −9.116 1.00 14.32 O HETATM 2387 O HOH W 34 −21.239 28.606 14.850 1.00 15.96 O HETATM 2388 O HOH W 35 −24.773 29.548 −12.422 1.00 15.43 O HETATM 2389 O HOH W 36 −20.822 20.806 −11.819 1.00 14.61 O HETATM 2390 O HOH W 37 −9.275 15.936 −22.055 1.00 14.71 O HETATM 2391 O HOH W 38 −20.594 14.589 13.855 1.00 17.78 O HETATM 2392 O HOH W 39 5.208 15.094 −10.204 1.00 16.41 O HETATM 2393 O HOH W 40 −20.072 5.193 14.956 1.00 15.13 O HETATM 2394 O HOH W 41 −13.159 26.020 −13.404 1.00 16.62 O HETATM 2395 O HOH W 42 −26.282 23.518 16.511 1.00 20.84 O HETATM 2396 O HOH W 43 −10.302 34.220 3.868 1.00 18.17 O HETATM 2397 O HOH W 44 −1.928 29.772 2.061 1.00 15.99 O HETATM 2398 O HOH W 45 −2.744 28.535 7.126 1.00 19.79 O HETATM 2399 O HOH W 46 −5.515 17.879 −17.351 1.00 19.09 O HETATM 2400 O HOH W 47 −12.817 5.509 −17.997 1.00 18.20 O HETATM 2401 O HOH W 48 −14.357 31.242 −7.410 1.00 17.27 O HETATM 2402 O HOH W 49 −14.923 14.930 −21.033 1.00 17.02 O HETATM 2403 O HOH W 50 −9.458 23.156 9.139 1.00 21.87 O HETATM 2404 O HOH W 51 0.257 31.525 −7.428 1.00 18.65 O HETATM 2405 O HOH W 52 −25.578 20.460 −14.720 1.00 18.62 O HETATM 2406 O HOH W 53 −20.547 12.617 −23.501 1.00 20.46 O HETATM 2407 O HOH W 54 −23.950 26.787 −18.563 1.00 17.02 O HETATM 2408 O HOH W 55 −14.696 9.975 −8.189 1.00 19.62 O HETATM 2409 O HOH W 56 −25.051 13.877 −15.630 1.00 17.92 O HETATM 2410 O HOH W 57 −8.564 7.506 −8.708 1.00 18.44 O HETATM 2411 O HOH W 58 −26.198 31.102 −16.423 1.00 16.37 O HETATM 2412 O HOH W 59 −37.176 12.986 −4.281 1.00 21.18 O HETATM 2413 O HOH W 60 −0.408 19.850 −9.658 1.00 20.96 O HETATM 2414 O HOH W 61 −27.390 2.115 −8.137 1.00 20.41 O HETATM 2415 O HOH W 62 −18.345 0.114 10.794 1.00 19.73 O HETATM 2416 O HOH W 63 −7.560 17.472 11.844 1.00 20.82 O HETATM 2417 O HOH W 64 −10.060 27.021 −17.033 1.00 19.15 O HETATM 2418 O HOH W 65 −11.889 25.550 −15.567 1.00 17.58 O HETATM 2419 O HOH W 66 −0.270 32.535 −4.292 1.00 23.13 O HETATM 2420 O HOH W 67 −2.409 13.621 −0.840 1.00 20.38 O HETATM 2421 O HOH W 68 −26.262 31.478 −13.675 1.00 20.59 O HETATM 2422 O HOH W 69 −28.229 3.738 −13.695 1.00 21.62 O HETATM 2423 O HOH W 70 −31.712 27.290 −6.129 1.00 18.31 O HETATM 2424 O HOH W 71 −6.300 21.250 −19.853 1.00 16.05 O HETATM 2425 O HOH W 72 −28.617 2.134 3.116 1.00 24.09 O HETATM 2426 O HOH W 73 −6.265 12.778 −21.032 1.00 20.88 O HETATM 2427 O HOH W 74 −5.345 21.003 −9.170 1.00 20.95 O HETATM 2428 O HOH W 75 −13.672 40.032 1.481 1.00 20.82 O HETATM 2429 O HOH W 76 3.970 33.284 −8.733 1.00 21.52 O HETATM 2430 O HOH W 77 −27.601 3.453 −1.085 1.00 19.94 O HETATM 2431 O HOH W 78 −16.463 32.339 14.904 1.00 20.41 O HETATM 2432 O HOH W 79 −30.731 36.819 4.054 1.00 22.74 O HETATM 2433 O HOH W 80 −10.846 1.831 −7.270 1.00 21.37 O HETATM 2434 O HOH W 81 −27.313 22.838 −11.310 1.00 24.03 O HETATM 2435 O HOH W 82 −15.217 31.789 −19.315 1.00 23.88 O HETATM 2436 O HOH W 83 −33.912 16.169 −9.052 1.00 22.87 O HETATM 2437 O HOH W 84 −20.209 −1.679 12.463 1.00 21.35 O HETATM 2438 O HOH W 85 −5.913 10.247 −9.105 1.00 22.32 O HETATM 2439 O HOH W 86 −0.959 17.408 2.354 1.00 20.98 O HETATM 2440 O HOH W 87 −10.503 38.192 0.316 1.00 24.62 O HETATM 2441 O HOH W 88 −32.112 7.871 −10.243 1.00 21.94 O HETATM 2442 O HOH W 89 −13.180 25.290 −17.756 1.00 19.54 O HETATM 2443 O HOH W 90 −7.804 19.778 −13.041 1.00 24.06 O HETATM 2444 O HOH W 91 −33.427 27.311 −4.139 1.00 23.94 O HETATM 2445 O HOH W 92 −12.229 34.941 5.552 1.00 22.55 O HETATM 2446 O HOH W 93 −40.268 22.945 5.322 1.00 24.66 O HETATM 2447 O HOH W 94 −11.361 −0.276 9.385 1.00 24.33 O HETATM 2448 O HOH W 95 −5.594 12.673 4.154 1.00 21.98 O HETATM 2449 O HOH W 96 −30.277 8.393 11.189 1.00 23.95 O HETATM 2450 O HOH W 97 −3.885 31.646 2.132 1.00 23.08 O HETATM 2451 O HOH W 98 −15.349 37.712 −10.155 1.00 22.78 O HETATM 2452 O HOH W 99 −27.793 8.032 10.121 1.00 21.52 O HETATM 2453 O HOH W 100 1.726 25.595 −13.323 1.00 24.61 O HETATM 2454 O HOH W 101 −4.022 23.204 −10.234 1.00 23.85 O HETATM 2455 O HOH W 102 −0.283 27.133 5.706 1.00 27.07 O HETATM 2456 O HOH W 103 −17.612 12.195 13.686 1.00 22.47 O HETATM 2457 O HOH W 104 −20.617 38.511 11.379 1.00 22.85 O HETATM 2458 O HOH W 105 −12.949 21.628 −20.519 1.00 22.65 O HETATM 2459 O HOH W 106 −8.950 13.120 −21.827 1.00 24.72 O HETATM 2460 O HOH W 107 −24.860 6.230 −19.460 1.00 22.27 O HETATM 2461 O HOH W 108 −19.286 25.663 −23.124 1.00 24.09 O HETATM 2462 O HOH W 109 −4.483 32.563 −11.039 1.00 27.41 O HETATM 2463 O HOH W 110 −29.993 33.249 4.804 1.00 24.16 O HETATM 2464 O HOH W 111 12.207 32.873 0.335 1.00 25.14 O HETATM 2465 O HOH W 112 −34.084 27.205 19.146 1.00 21.94 O HETATM 2466 O HOH W 113 −26.787 5.452 10.766 1.00 22.13 O HETATM 2467 O HOH W 114 1.550 16.445 −12.673 1.00 29.27 O HETATM 2468 O HOH W 115 0.773 22.236 −9.903 1.00 21.44 O HETATM 2469 O HOH W 116 −15.044 17.209 −22.620 1.00 21.87 O HETATM 2470 O HOH W 117 −25.901 32.220 9.915 1.00 21.85 O HETATM 2471 O HOH W 118 −15.258 40.579 −2.244 1.00 27.72 O HETATM 2472 O HOH W 119 −7.794 30.680 −9.041 1.00 23.66 O HETATM 2473 O HOH W 120 −18.635 35.461 −11.584 1.00 24.31 O HETATM 2474 O HOH W 121 −26.081 16.654 −25.505 1.00 22.43 O HETATM 2475 O HOH W 122 −9.221 9.291 −15.768 1.00 27.18 O HETATM 2476 O HOH W 123 −28.859 32.651 −7.827 1.00 31.44 O HETATM 2477 O HOH W 124 −1.147 11.892 −2.485 1.00 25.34 O HETATM 2478 O HOH W 125 −16.717 23.990 −23.206 1.00 22.72 O HETATM 2479 O HOH W 126 −16.904 27.933 15.146 1.00 28.48 O HETATM 2480 O HOH W 127 −24.881 −0.157 −9.675 1.00 30.44 O HETATM 2481 O HOH W 128 −12.528 32.808 −13.738 1.00 23.97 O HETATM 2482 O HOH W 129 −31.526 33.432 −4.910 1.00 29.01 O HETATM 2483 O HOH W 130 −10.048 37.820 −7.038 1.00 29.37 O HETATM 2484 O HOH W 131 −11.867 19.403 12.228 1.00 29.42 O HETATM 2485 O HOH W 132 −37.133 10.668 3.881 1.00 30.27 O HETATM 2486 O HOH W 133 −19.747 3.815 −16.456 1.00 27.29 O HETATM 2487 O HOH W 134 −7.880 35.404 −6.844 1.00 24.86 O HETATM 2488 O HOH W 135 −8.998 3.716 −9.036 1.00 28.14 O HETATM 2489 O HOH W 136 −2.967 12.137 4.048 1.00 26.40 O HETATM 2490 O HOH W 137 −17.049 39.326 −11.678 1.00 25.80 O HETATM 2491 O HOH W 138 −10.257 −2.109 −12.040 1.00 29.56 O HETATM 2492 O HOH W 139 −26.119 34.050 −13.125 1.00 25.74 O HETATM 2493 O HOH W 140 −16.994 38.359 14.121 1.00 32.67 O HETATM 2494 O HOH W 141 −10.346 37.403 −10.034 1.00 28.07 O HETATM 2495 O HOH W 142 6.226 22.804 −1.176 1.00 26.21 O HETATM 2496 O HOH W 143 −7.855 32.548 9.121 1.00 31.08 O HETATM 2497 O HOH W 144 −38.520 18.008 −5.332 1.00 28.74 O HETATM 2498 O HOH W 145 0.863 30.021 −14.155 1.00 25.22 O HETATM 2499 O HOH W 146 −14.539 12.832 −22.506 1.00 34.74 O HETATM 2500 O HOH W 147 −9.685 35.266 7.783 1.00 39.75 O HETATM 2501 O HOH W 148 −4.940 15.663 −7.095 1.00 28.86 O HETATM 2502 O HOH W 149 −19.875 12.007 14.866 1.00 29.93 O HETATM 2503 O HOH W 150 −25.128 −0.534 −5.095 1.00 28.37 O HETATM 2504 O HOH W 151 −1.385 12.790 1.731 1.00 27.27 O HETATM 2505 O HOH W 152 −28.589 35.688 −8.140 1.00 29.37 O HETATM 2506 O HOH W 153 −39.946 16.242 11.666 1.00 27.63 O HETATM 2507 O HOH W 154 −12.005 32.563 12.899 1.00 28.89 O HETATM 2508 O HOH W 155 −32.382 11.270 10.718 1.00 27.03 O HETATM 2509 O HOH W 156 −6.547 26.498 11.420 1.00 26.38 O HETATM 2510 O HOH W 157 −15.098 4.994 −20.108 1.00 30.09 O HETATM 2511 O HOH W 158 −40.304 25.037 6.932 1.00 29.28 O HETATM 2512 O HOH W 159 −19.654 42.452 −11.933 1.00 28.67 O HETATM 2513 O HOH W 160 7.165 33.655 −14.239 1.00 29.40 O HETATM 2514 O HOH W 161 −29.918 4.810 −15.685 1.00 30.16 O HETATM 2515 O HOH W 162 10.935 23.184 −6.110 1.00 32.43 O HETATM 2516 O HOH W 163 −26.145 2.186 1.054 1.00 36.44 O HETATM 2517 O HOH W 164 −34.339 6.200 −6.038 1.00 31.60 O HETATM 2518 O HOH W 165 −7.577 23.852 11.873 1.00 37.15 O HETATM 2519 O HOH W 166 −28.374 17.766 15.757 1.00 33.08 O HETATM 2520 O HOH W 167 −8.878 30.353 10.450 1.00 33.65 O HETATM 2521 O HOH W 168 −39.240 24.455 13.603 1.00 32.18 O HETATM 2522 O HOH W 169 −5.259 32.467 −14.521 1.00 30.28 O HETATM 2523 O HOH W 170 −19.002 44.014 −6.429 1.00 36.88 O HETATM 2524 O HOH W 171 −41.472 23.045 −1.746 1.00 34.68 O HETATM 2525 O HOH W 172 −41.240 17.380 −0.287 1.00 30.69 O HETATM 2526 O HOH W 173 −18.871 43.325 −2.077 1.00 32.89 O HETATM 2527 O HOH W 174 −15.823 41.421 2.253 1.00 29.64 O HETATM 2528 O HOH W 175 −7.050 21.485 −11.124 1.00 32.96 O HETATM 2529 O HOH W 176 −37.741 26.386 −1.056 1.00 29.25 O HETATM 2530 O HOH W 177 −37.633 14.168 12.267 1.00 41.58 O HETATM 2531 O HOH W 178 −36.152 30.566 14.397 1.00 32.08 O HETATM 2532 O HOH W 179 −16.547 10.926 −22.860 1.00 29.03 O HETATM 2533 O HOH W 180 −41.727 23.706 9.092 1.00 33.88 O HETATM 2534 O HOH W 181 6.999 23.263 −12.013 1.00 36.81 O HETATM 2535 O HOH W 182 −17.044 8.041 −22.415 1.00 38.12 O HETATM 2536 O HOH W 183 −35.338 12.042 10.329 1.00 31.94 O HETATM 2537 O HOH W 184 2.050 23.137 −12.328 1.00 30.75 O HETATM 2538 O HOH W 185 −19.726 45.933 −2.467 1.00 38.74 O HETATM 2539 O HOH W 186 −0.301 9.788 −9.818 1.00 33.75 O HETATM 2540 O HOH W 187 −5.231 11.780 14.591 1.00 34.83 O HETATM 2541 O HOH W 188 −14.916 41.932 5.514 1.00 41.07 O HETATM 2542 O HOH W 189 −42.696 19.572 −0.424 1.00 32.59 O HETATM 2543 O HOH W 190 −0.895 14.955 4.198 1.00 36.30 O HETATM 2544 O HOH W 191 −18.995 3.659 −13.597 1.00 34.12 O HETATM 2545 O HOH W 192 −37.998 28.389 15.014 1.00 31.37 O HETATM 2546 O HOH W 193 −30.890 10.641 13.026 1.00 32.22 O HETATM 2547 O HOH W 194 −11.626 11.766 −21.687 1.00 36.98 O HETATM 2548 O HOH W 195 −14.658 39.550 −8.121 1.00 38.81 O HETATM 2549 O HOH W 196 −29.019 13.051 14.830 1.00 36.98 O HETATM 2550 O HOH W 197 −4.504 18.598 −10.348 1.00 38.67 O HETATM 2551 O HOH W 198 −0.549 14.853 −12.387 1.00 44.66 O HETATM 2552 O HOH W 199 −4.956 22.211 −15.525 1.00 36.99 O HETATM 2553 O HOH W 200 −4.889 15.947 −10.022 1.00 35.93 O HETATM 2554 O HOH W 201 −23.924 21.128 −22.907 1.00 33.50 O HETATM 2555 O HOH W 202 −15.047 33.244 −10.368 1.00 35.92 O HETATM 2556 O HOH W 203 −38.527 11.133 10.261 1.00 37.83 O HETATM 2557 O HOH W 204 −9.009 31.981 −16.860 1.00 31.39 O HETATM 2558 O HOH W 205 −38.191 21.671 15.013 1.00 36.15 O HETATM 2559 O HOH W 206 −18.868 10.333 −23.932 1.00 46.13 O HETATM 2560 O HOH W 207 −35.132 25.919 −6.614 1.00 52.07 O HETATM 2561 O HOH W 208 −27.841 21.763 −15.855 1.00 41.85 O HETATM 2562 O HOH W 209 −34.644 43.404 −1.444 1.00 38.81 O HETATM 2563 O HOH W 210 −30.201 3.894 −11.360 1.00 37.63 O HETATM 2564 O HOH W 211 −22.748 49.399 −4.251 1.00 36.11 O HETATM 2565 O HOH W 212 −1.483 14.264 8.431 1.00 41.49 O HETATM 2566 O HOH W 213 −23.051 11.708 −21.920 1.00 36.32 O HETATM 2567 O HOH W 214 1.620 18.299 2.516 1.00 40.18 O HETATM 2568 O HOH W 215 −24.103 43.355 −12.751 1.00 37.49 O HETATM 2569 O HOH W 216 −26.738 0.134 −2.192 1.00 40.25 O HETATM 2570 O HOH W 217 11.242 21.332 −4.106 1.00 38.90 O HETATM 2571 O HOH W 218 −14.341 33.661 14.752 1.00 43.39 O HETATM 2572 O HOH W 219 −42.307 15.549 8.867 1.00 48.18 O HETATM 2573 O HOH W 220 −36.432 28.737 −0.897 1.00 39.64 O HETATM 2574 O HOH W 221 −25.417 28.494 −16.695 1.00 29.40 O HETATM 2575 O HOH W 222 −19.511 43.409 6.951 1.00 28.17 O HETATM 2576 O HOH W 223 −10.123 16.512 −24.639 1.00 31.70 O HETATM 2577 O HOH W 224 −25.245 45.166 −11.086 1.00 29.38 O HETATM 2578 O HOH W 225 −23.616 45.957 4.604 1.00 46.22 O HETATM 2579 O HOH W 226 −4.587 19.737 −15.634 1.00 37.60 O HETATM 2580 O HOH W 227 −24.137 7.274 −21.752 1.00 39.86 O HETATM 2581 O HOH W 228 −12.824 13.338 18.692 1.00 35.98 O HETATM 2582 O HOH W 229 −0.643 15.774 −0.049 1.00 38.98 O HETATM 2583 O HOH W 230 −19.204 39.608 13.339 1.00 44.88 O HETATM 2584 O HOH W 231 −40.196 18.266 13.870 1.00 39.93 O HETATM 2585 O HOH W 232 −18.669 36.100 15.012 1.00 40.93 O HETATM 2586 O HOH W 233 −29.410 26.628 −9.566 1.00 40.47 O HETATM 2587 O HOH W 234 −30.809 34.598 −7.203 1.00 42.41 O HETATM 2588 O HOH W 235 −22.479 15.485 19.837 1.00 46.47 O HETATM 2589 O HOH W 236 −22.471 4.871 16.342 1.00 44.82 O HETATM 2590 O HOH W 237 −34.347 29.636 −4.151 1.00 41.68 O HETATM 2591 O HOH W 238 −36.466 16.190 −8.418 1.00 38.78 O HETATM 2592 O HOH W 239 −17.832 41.337 −3.943 1.00 40.59 O HETATM 2593 O HOH W 240 −5.599 3.373 1.035 1.00 37.39 O HETATM 2594 O HOH W 241 −31.315 43.021 6.641 1.00 44.12 O HETATM 2595 O HOH W 242 −0.730 9.262 −1.771 1.00 40.88 O HETATM 2596 O HOH W 243 4.759 11.224 −6.950 1.00 47.42 O HETATM 2597 O HOH W 244 −10.999 3.648 −16.952 1.00 46.46 O HETATM 2598 O HOH W 245 −5.652 21.836 12.464 1.00 42.81 O HETATM 2599 O HOH W 246 −14.550 10.917 18.018 1.00 41.09 O HETATM 2600 O HOH W 247 −4.947 4.565 −7.195 1.00 46.09 O HETATM 2601 O HOH W 248 −24.134 51.667 −5.997 1.00 46.36 O HETATM 2602 O HOH W 249 −37.327 13.552 −6.997 1.00 53.05 O HETATM 2603 O HOH W 250 0.506 22.694 3.267 1.00 47.90 O HETATM 2604 O HOH W 251 −13.591 16.310 −24.807 1.00 50.85 O HETATM 2605 O HOH W 252 −9.018 7.158 −17.757 1.00 46.53 O HETATM 2606 O HOH W 253 −26.754 28.420 −10.600 1.00 29.06 O HETATM 2607 O HOH W 254 −18.410 44.305 9.205 1.00 29.63 O HETATM 2608 O HOH W 255 −32.584 10.434 −11.160 1.00 41.22 O HETATM 2609 O HOH W 256 −16.091 1.690 16.162 1.00 36.96 O HETATM 2610 O HOH W 257 −4.505 9.349 11.016 1.00 39.86 O HETATM 2611 O HOH W 258 −40.947 18.159 −3.757 1.00 43.42 O HETATM 2612 O HOH W 259 0.000 24.141 −15.150 1.00 38.32 O HETATM 2613 O HOH W 260 −44.582 24.137 6.565 1.00 51.92 O HETATM 2614 O HOH W 261 −35.232 13.693 −8.515 1.00 55.39 O HETATM 2615 O HOH W 262 −29.872 45.235 6.694 1.00 17.67 O HETATM 2616 O HOH W 263 −27.113 45.109 −0.458 1.00 22.65 O HETATM 2617 O HOH W 264 −25.323 47.035 2.382 1.00 28.79 O HETATM 2618 O HOH W 265 0.000 26.981 −15.150 1.00 32.82 O HETATM 2619 O HOH W 266 −18.156 20.703 −27.017 1.00 35.61 O HETATM 2620 O HOH W 267 −37.722 10.433 −4.365 1.00 45.06 O HETATM 2621 O HOH W 268 −16.805 35.390 −9.635 1.00 40.40 O HETATM 2622 O HOH W 269 −16.918 18.529 −26.281 1.00 39.96 O HETATM 2623 O HOH W 270 −13.491 38.406 −6.271 1.00 39.29 O HETATM 2624 O HOH W 271 −8.148 20.081 11.966 1.00 44.03 O HETATM 2625 O HOH W 272 −6.821 1.644 3.126 1.00 40.41 O HETATM 2626 O HOH W 273 −18.313 5.740 −22.619 1.00 47.63 O HETATM 2627 O HOH W 274 −13.103 2.644 −18.422 1.00 45.18 O HETATM 2628 O HOH W 275 −0.862 26.991 8.197 1.00 49.93 O HETATM 2629 O HOH W 276 −12.480 35.715 13.919 1.00 48.53 O HETATM 2630 O HOH W 277 −6.665 2.991 −5.698 1.00 47.86 O HETATM 2631 O HOH W 278 −6.235 34.850 −10.896 1.00 49.10 O HETATM 2632 O HOH W 279 −15.224 26.534 14.107 1.00 34.50 O HETATM 2633 O HOH W 280 −26.785 17.717 −14.048 1.00 32.29 O HETATM 2634 O HOH W 281 −10.359 3.127 −14.054 1.00 35.76 O HETATM 2635 O HOH W 282 −9.964 34.823 −10.668 1.00 36.66 O HETATM 2636 O HOH W 283 −10.871 37.987 5.889 1.00 39.81 O HETATM 2637 O HOH W 284 −26.828 12.543 −16.696 1.00 39.23 O HETATM 2638 O HOH W 285 −28.134 16.073 −12.715 1.00 39.10 O HETATM 2639 O HOH W 286 −8.308 33.139 −8.609 1.00 41.47 O HETATM 2640 O HOH W 287 4.685 22.519 −12.295 1.00 43.15 O HETATM 2641 O HOH W 288 −6.455 17.658 −13.209 1.00 43.22 O HETATM 2642 O HOH W 289 −29.264 4.527 11.185 1.00 38.52 O HETATM 2643 O HOH W 290 1.948 31.540 −15.946 1.00 42.96 O HETATM 2644 O HOH W 291 −28.001 47.360 −9.030 1.00 42.25 O HETATM 2645 O HOH W 292 −21.578 9.488 15.696 1.00 48.22 O HETATM 2646 O HOH W 293 −36.209 19.343 −11.413 1.00 43.75 O HETATM 2647 O HOH W 294 0.319 29.212 4.405 1.00 42.45 O HETATM 2648 O HOH W 295 −43.593 18.340 3.119 1.00 44.30 O HETATM 2649 O HOH W 296 −8.690 9.796 −18.360 1.00 48.63 O HETATM 2650 O HOH W 297 −13.183 20.728 −23.025 1.00 42.14 O HETATM 2651 O HOH W 298 −28.554 16.113 −23.692 1.00 44.64 O HETATM 2652 O HOH W 299 −11.671 39.418 10.822 1.00 44.26 O HETATM 2653 O HOH W 300 −7.956 4.305 −13.456 1.00 46.03 O HETATM 2654 O HOH W 301 −39.821 23.326 16.353 1.00 43.78 O HETATM 2655 O HOH W 302 −13.526 31.064 14.928 1.00 53.12 O HETATM 2656 O HOH W 303 −17.878 33.786 16.873 1.00 50.15 O HETATM 2657 O HOH W 304 −33.678 7.362 −8.182 1.00 49.39 O HETATM 2658 O HOH W 305 −11.597 39.294 −8.859 1.00 53.94 O HETATM 2659 O HOH W 306 2.882 29.239 3.191 1.00 45.89 O HETATM 2660 O HOH W 307 −38.649 20.156 −7.082 1.00 49.36 O HETATM 2661 O HOH W 308 −40.591 26.658 0.275 1.00 43.29 O HETATM 2662 O HOH W 309 −6.537 4.311 13.825 1.00 47.40 O HETATM 2663 O HOH W 310 −5.558 35.013 −13.517 1.00 48.80 O HETATM 2664 O HOH W 311 −28.826 11.425 −15.322 1.00 49.38 O HETATM 2665 O HOH W 312 −38.320 28.225 17.606 1.00 55.51 O HETATM 2666 O HOH W 313 −23.593 4.828 13.752 1.00 27.36 O HETATM 2667 O HOH W 314 −23.921 26.545 −16.243 1.00 34.27 O HETATM 2668 O HOH W 315 −22.322 11.653 14.462 1.00 34.83 O HETATM 2669 O HOH W 316 −12.651 34.045 −11.232 1.00 31.40 O HETATM 2670 O HOH W 317 −11.298 29.991 11.215 1.00 37.94 O HETATM 2671 O HOH W 318 −22.524 14.427 −23.824 1.00 34.38 O HETATM 2672 O HOH W 319 −17.894 26.130 16.911 1.00 40.42 O HETATM 2673 O HOH W 320 −30.095 30.303 9.084 1.00 43.47 O HETATM 2674 O HOH W 321 −13.730 28.546 14.642 1.00 45.76 O HETATM 2675 O HOH W 322 0.192 20.485 4.996 1.00 42.15 O HETATM 2676 O HOH W 323 8.773 19.721 −2.795 1.00 41.00 O HETATM 2677 O HOH W 324 −24.325 35.749 −12.402 1.00 41.84 O HETATM 2678 O HOH W 325 −24.805 13.589 −22.690 1.00 42.74 O HETATM 2679 O HOH W 326 −16.673 23.836 17.169 1.00 42.32 O HETATM 2680 O HOH W 327 −26.618 15.414 −14.762 1.00 52.87 O HETATM 2681 O HOH W 328 −17.876 41.703 11.298 1.00 40.21 O HETATM 2682 O HOH W 329 2.710 12.479 −3.493 1.00 41.71 O HETATM 2683 O HOH W 330 −40.522 22.831 11.667 1.00 40.68 O HETATM 2684 O HOH W 331 −5.318 8.894 −11.975 1.00 45.24 O HETATM 2685 O HOH W 332 6.465 34.844 −5.820 1.00 41.37 O HETATM 2686 O HOH W 333 −7.294 7.847 −13.196 1.00 46.21 O HETATM 2687 O HOH W 334 −27.575 −1.555 −9.482 1.00 43.31 O HETATM 2688 O HOH W 335 −16.302 44.157 6.300 1.00 50.65 O HETATM 2689 O HOH W 336 7.324 25.112 −0.042 1.00 46.30 O HETATM 2690 O HOH W 337 −25.386 14.745 −27.433 1.00 48.90 O HETATM 2691 O HOH W 338 −11.898 7.106 −19.877 1.00 48.25 O HETATM 2692 O HOH W 339 −6.543 5.813 −9.614 1.00 50.85 O HETATM 2693 O HOH W 340 −24.469 1.696 −2.733 1.00 49.67 O HETATM 2694 O HOH W 341 −25.761 37.027 −10.672 1.00 43.85 O HETATM 2695 O HOH W 342 −37.486 7.329 −1.731 1.00 48.83 O HETATM 2696 O HOH W 343 −17.291 4.085 16.803 1.00 48.72 O HETATM 2697 O HOH W 344 −14.036 26.435 −22.926 1.00 43.49 O HETATM 2698 O HOH W 345 0.692 30.664 2.086 1.00 53.06 O HETATM 2699 O HOH W 346 −41.805 14.047 −3.004 1.00 45.34 O HETATM 2700 O HOH W 347 −5.313 18.738 12.526 1.00 56.10 O HETATM 2701 O HOH W 348 −15.979 2.222 −18.286 1.00 52.97 O HETATM 2702 O HOH W 349 12.845 27.550 2.215 1.00 51.89 O HETATM 2703 O HOH W 350 −24.703 2.114 13.280 1.00 52.54 O HETATM 2704 O HOH W 351 −13.629 8.385 17.755 1.00 53.31 O HETATM 2705 O HOH W 352 0.600 10.756 1.065 1.00 52.20 O HETATM 2706 O HOH W 353 −6.584 3.294 −8.664 1.00 58.25 O HETATM 2707 O HOH W 354 −19.526 1.509 −15.069 1.00 58.64 O HETATM 2708 O HOH W 355 −37.744 8.976 −6.842 1.00 49.38 O HETATM 2709 O HOH W 356 11.571 31.022 2.199 1.00 49.80 O HETATM 2710 O HOH W 357 −5.947 36.986 −4.732 1.00 50.31 O HETATM 2711 O HOH W 358 −15.405 41.052 11.474 1.00 51.49 O HETATM 2712 O HOH W 359 −12.833 40.449 −4.727 1.00 51.48 O HETATM 2713 O HOH W 360 −5.438 1.935 −3.550 1.00 50.92 O HETATM 2714 O HOH W 361 −10.249 0.894 −12.528 1.00 59.44 O HETATM 2715 O HOH W 362 −31.963 40.849 5.308 1.00 56.17 O HETATM 2716 O HOH W 363 −20.396 19.502 −28.110 1.00 57.97 O HETATM 2717 O HOH W 364 −38.545 15.892 −6.873 1.00 53.86 O HETATM 2718 O HOH W 365 −8.651 36.740 4.818 1.00 56.42 O HETATM 2719 O HOH W 366 −16.900 45.179 −0.086 1.00 57.28 O HETATM 2720 O HOH W 367 −15.600 42.705 −0.411 1.00 53.55 O HETATM 2721 O HOH W 368 −1.122 22.193 −13.088 1.00 50.00 O HETATM 2722 O HOH W 369 −3.015 2.725 5.944 1.00 49.17 O HETATM 2723 O HOH W 370 −32.840 41.664 3.046 1.00 55.05 O HETATM 2724 O HOH W 371 −31.332 6.082 11.720 1.00 55.05 O HETATM 2725 O HOH W 372 −5.263 32.737 9.359 1.00 53.35 O HETATM 2726 O HOH W 373 −17.185 11.511 17.118 1.00 55.25 O HETATM 2727 O HOH W 374 −9.075 41.015 −9.468 1.00 55.28 O HETATM 2728 O HOH W 375 −2.683 7.946 9.076 1.00 55.07 O HETATM 2729 O HOH W 376 7.720 16.995 −3.341 1.00 52.87 O HETATM 2730 O HOH W 377 −4.253 13.777 −12.953 1.00 51.97 O END

TABLE 7 CRYST1 128.605 72.028 65.241 90.00 93.89 90.00 C 1 2 1 SCALE1 0.007776 −0.000000 0.000529 0.00000 SCALE2 0.000000 0.013883 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015363 0.00000 ATOM 1 N PRO A 7 48.590 9.939 −13.655 1.00 42.38 N ATOM 2 CA PRO A 7 47.335 9.560 −14.312 1.00 42.38 C ATOM 3 C PRO A 7 46.165 10.267 −13.649 1.00 42.38 C ATOM 4 CB PRO A 7 47.247 8.043 −14.089 1.00 42.38 C ATOM 5 CG PRO A 7 48.591 7.620 −13.573 1.00 42.38 C ATOM 6 CD PRO A 7 49.172 8.826 −12.893 1.00 42.38 C ATOM 7 O PRO A 7 46.389 11.304 −13.019 1.00 42.38 O ATOM 8 N ARG A 8 44.956 9.721 −13.774 1.00 39.85 N ATOM 9 CA ARG A 8 43.761 10.386 −13.255 1.00 39.85 C ATOM 10 C ARG A 8 43.204 9.709 −11.991 1.00 39.85 C ATOM 11 CB ARG A 8 42.689 10.485 −14.345 1.00 39.85 C ATOM 12 CG ARG A 8 41.906 11.799 −14.337 1.00 39.85 C ATOM 13 CD ARG A 8 42.743 12.963 −14.880 1.00 39.85 C ATOM 14 NE ARG A 8 42.014 14.234 −14.896 1.00 39.85 N ATOM 15 CZ ARG A 8 41.184 14.608 −15.866 1.00 39.85 C ATOM 16 NH1 ARG A 8 40.967 13.802 −16.892 1.00 39.85 N ATOM 17 NH2 ARG A 8 40.561 15.780 −15.812 1.00 39.85 N ATOM 18 O ARG A 8 43.047 8.484 −11.943 1.00 39.85 O ATOM 19 N ARG A 9 42.910 10.527 −10.978 1.00 23.40 N ATOM 20 CA ARG A 9 42.492 10.067 −9.656 1.00 23.40 C ATOM 21 C ARG A 9 41.498 11.041 −9.023 1.00 23.40 C ATOM 22 O ARG A 9 41.444 12.220 −9.385 1.00 23.40 O ATOM 23 CB ARG A 9 43.703 9.985 −8.739 1.00 23.40 C ATOM 24 CG ARG A 9 44.946 9.489 −9.410 1.00 23.40 C ATOM 25 CD ARG A 9 46.175 10.149 −8.821 1.00 23.40 C ATOM 26 NE ARG A 9 47.328 9.259 −8.863 1.00 23.40 N ATOM 27 CZ ARG A 9 47.757 8.542 −7.829 1.00 23.40 C ATOM 28 NH1 ARG A 9 47.142 8.622 −6.654 1.00 23.40 N ATOM 29 NH2 ARG A 9 48.808 7.749 −7.969 1.00 23.40 N ATOM 30 N THR A 10 40.730 10.555 −8.052 1.00 25.63 N ATOM 31 CA THR A 10 39.797 11.404 −7.320 1.00 25.63 C ATOM 32 C THR A 10 40.563 12.566 −6.723 1.00 25.63 C ATOM 33 O THR A 10 41.786 12.531 −6.639 1.00 25.63 O ATOM 34 CB THR A 10 39.096 10.641 −6.168 1.00 25.63 C ATOM 35 OG1 THR A 10 39.990 10.504 −5.057 1.00 25.63 O ATOM 36 CG2 THR A 10 38.664 9.264 −6.615 1.00 25.63 C ATOM 37 N PRO A 11 39.846 13.612 −6.314 1.00 19.58 N ATOM 38 CA PRO A 11 40.493 14.666 −5.536 1.00 19.58 C ATOM 39 C PRO A 11 41.198 14.045 −4.348 1.00 19.58 C ATOM 40 O PRO A 11 42.303 14.465 −4.018 1.00 19.58 O ATOM 41 CB PRO A 11 39.317 15.514 −5.053 1.00 19.58 C ATOM 42 CG PRO A 11 38.281 15.322 −6.082 1.00 19.58 C ATOM 43 CD PRO A 11 38.425 13.897 −6.558 1.00 19.58 C ATOM 44 N GLN A 12 40.561 13.048 −3.731 1.00 37.33 N ATOM 45 CA GLN A 12 41.098 12.371 −2.551 1.00 37.33 C ATOM 46 C GLN A 12 42.140 11.323 −2.908 1.00 37.33 C ATOM 47 O GLN A 12 42.537 10.513 −2.066 1.00 37.33 O ATOM 48 CB GLN A 12 39.978 11.735 −1.730 1.00 37.33 C ATOM 49 CG GLN A 12 39.170 12.732 −0.918 1.00 37.33 C ATOM 50 CD GLN A 12 38.041 13.354 −1.716 1.00 37.33 C ATOM 51 OE1 GLN A 12 37.847 13.036 −2.890 1.00 37.33 O ATOM 52 NE2 GLN A 12 37.282 14.241 −1.076 1.00 37.33 N ATOM 53 N SER A 13 42.551 11.334 −4.171 1.00 13.69 N ATOM 54 CA SER A 13 43.746 10.627 −4.624 1.00 13.69 C ATOM 55 C SER A 13 43.515 9.168 −4.970 1.00 13.69 C ATOM 56 O SER A 13 44.444 8.376 −4.937 1.00 13.69 O ATOM 57 CB SER A 13 44.882 10.759 −3.599 1.00 13.69 C ATOM 58 OG SER A 13 45.123 12.126 −3.274 1.00 13.69 O ATOM 59 N ILE A 14 42.287 8.810 −5.318 1.00 7.31 N ATOM 60 CA ILE A 14 42.013 7.440 −5.720 1.00 7.31 C ATOM 61 C ILE A 14 41.958 7.331 −7.236 1.00 7.31 C ATOM 62 O ILE A 14 41.108 7.950 −7.863 1.00 7.31 O ATOM 63 CB ILE A 14 40.684 6.930 −5.144 1.00 7.31 C ATOM 64 CG1 ILE A 14 40.577 7.270 −3.657 1.00 7.31 C ATOM 65 CG2 ILE A 14 40.552 5.425 −5.360 1.00 7.31 C ATOM 66 CD1 ILE A 14 41.622 6.599 −2.800 1.00 7.31 C ATOM 67 N PRO A 15 42.873 6.544 −7.834 1.00 25.68 N ATOM 68 CA PRO A 15 42.886 6.332 −9.290 1.00 25.68 C ATOM 69 C PRO A 15 41.499 6.032 −9.852 1.00 25.68 C ATOM 70 O PRO A 15 40.942 4.967 −9.579 1.00 25.68 O ATOM 71 CB PRO A 15 43.796 5.114 −9.450 1.00 25.68 C ATOM 72 CG PRO A 15 44.752 5.227 −8.309 1.00 25.68 C ATOM 73 CD PRO A 15 43.977 5.830 −7.164 1.00 25.68 C ATOM 74 N TYR A 16 40.952 6.966 −10.628 1.00 43.94 N ATOM 75 CA TYR A 16 39.611 6.810 −11.190 1.00 43.94 C ATOM 76 C TYR A 16 39.482 5.526 −11.976 1.00 43.94 C ATOM 77 O TYR A 16 38.401 4.952 −12.052 1.00 43.94 O ATOM 78 CB TYR A 16 39.254 7.969 −12.118 1.00 43.94 C ATOM 79 CG TYR A 16 38.735 9.203 −11.424 1.00 43.94 C ATOM 80 CD1 TYR A 16 37.519 9.190 −10.753 1.00 43.94 C ATOM 81 CD2 TYR A 16 39.452 10.390 −11.464 1.00 43.94 C ATOM 82 CE1 TYR A 16 37.041 10.324 −10.126 1.00 43.94 C ATOM 83 CE2 TYR A 16 38.983 11.531 −10.844 1.00 43.94 C ATOM 84 CZ TYR A 16 37.780 11.498 −10.175 1.00 43.94 C ATOM 85 OH TYR A 16 37.323 12.643 −9.556 1.00 43.94 O ATOM 86 N GLN A 17 40.587 5.094 −12.575 1.00 33.47 N ATOM 87 CA GLN A 17 40.620 3.868 −13.370 1.00 33.47 C ATOM 88 C GLN A 17 39.950 2.682 −12.648 1.00 33.47 C ATOM 89 O GLN A 17 39.506 1.725 −13.283 1.00 33.47 O ATOM 90 CB GLN A 17 42.069 3.504 −13.734 1.00 33.47 C ATOM 91 CG GLN A 17 42.953 4.660 −14.199 1.00 33.47 C ATOM 92 CD GLN A 17 44.273 4.180 −14.795 1.00 33.47 C ATOM 93 OE1 GLN A 17 44.306 3.661 −15.911 1.00 33.47 O ATOM 94 NE2 GLN A 17 45.368 4.368 −14.057 1.00 33.47 N ATOM 95 N ASP A 18 39.875 2.764 −11.320 1.00 31.00 N ATOM 96 CA ASP A 18 39.381 1.665 −10.497 1.00 31.00 C ATOM 97 C ASP A 18 37.989 1.939 −9.931 1.00 31.00 C ATOM 98 O ASP A 18 37.378 1.065 −9.302 1.00 31.00 O ATOM 99 CB ASP A 18 40.354 1.409 −9.351 1.00 31.00 C ATOM 100 CG ASP A 18 41.798 1.609 −9.760 1.00 31.00 C ATOM 101 OD1 ASP A 18 42.222 1.034 −10.787 1.00 31.00 O ATOM 102 OD2 ASP A 18 42.510 2.343 −9.047 1.00 31.00 O ATOM 103 N LEU A 19 37.494 3.155 −10.151 1.00 22.04 N ATOM 104 CA LEU A 19 36.181 3.555 −9.644 1.00 22.04 C ATOM 105 C LEU A 19 35.150 3.666 −10.768 1.00 22.04 C ATOM 106 O LEU A 19 35.515 3.750 −11.937 1.00 22.04 O ATOM 107 CB LEU A 19 36.278 4.879 −8.879 1.00 22.04 C ATOM 108 CG LEU A 19 37.230 4.942 −7.683 1.00 22.04 C ATOM 109 CD1 LEU A 19 37.097 6.284 −6.970 1.00 22.04 C ATOM 110 CD2 LEU A 19 36.981 3.778 −6.729 1.00 22.04 C ATOM 111 N PRO A 20 33.853 3.654 −10.415 1.00 30.72 N ATOM 112 CA PRO A 20 32.789 3.806 −11.409 1.00 30.72 C ATOM 113 C PRO A 20 32.717 5.256 −11.833 1.00 30.72 C ATOM 114 O PRO A 20 32.847 6.140 −10.993 1.00 30.72 O ATOM 115 CB PRO A 20 31.515 3.439 −10.633 1.00 30.72 C ATOM 116 CG PRO A 20 31.971 2.882 −9.329 1.00 30.72 C ATOM 117 CD PRO A 20 33.308 3.482 −9.062 1.00 30.72 C ATOM 118 N HIS A 21 32.498 5.516 −13.110 1.00 20.94 N ATOM 119 CA HIS A 21 32.541 6.890 −13.555 1.00 20.94 C ATOM 120 C HIS A 21 32.053 7.092 −14.978 1.00 20.94 C ATOM 121 O HIS A 21 31.573 6.167 −15.628 1.00 20.94 O ATOM 122 CB HIS A 21 33.981 7.390 −13.455 1.00 20.94 C ATOM 123 CG HIS A 21 34.976 6.527 −14.174 1.00 20.94 C ATOM 124 ND1 HIS A 21 36.226 6.246 −13.663 1.00 20.94 N ATOM 125 CD2 HIS A 21 34.907 5.883 −15.365 1.00 20.94 C ATOM 126 CE1 HIS A 21 36.884 5.474 −14.509 1.00 20.94 C ATOM 127 NE2 HIS A 21 36.105 5.236 −15.548 1.00 20.94 N ATOM 128 N LEU A 22 32.163 8.337 −15.425 1.00 22.69 N ATOM 129 CA LEU A 22 32.162 8.696 −16.838 1.00 22.69 C ATOM 130 C LEU A 22 32.580 10.144 −16.916 1.00 22.69 C ATOM 131 O LEU A 22 32.784 10.779 −15.877 1.00 22.69 O ATOM 132 CB LEU A 22 30.805 8.486 −17.515 1.00 22.69 C ATOM 133 CG LEU A 22 29.489 8.863 −16.834 1.00 22.69 C ATOM 134 CD1 LEU A 22 29.647 10.059 −15.906 1.00 22.69 C ATOM 135 CD2 LEU A 22 28.421 9.120 −17.897 1.00 22.69 C ATOM 136 N VAL A 23 32.700 10.674 −18.131 1.00 6.20 N ATOM 137 CA VAL A 23 33.280 12.011 −18.282 1.00 6.20 C ATOM 138 C VAL A 23 32.324 13.154 −18.654 1.00 6.20 C ATOM 139 O VAL A 23 31.842 13.261 −19.785 1.00 6.20 O ATOM 140 CB VAL A 23 34.527 12.024 −19.206 1.00 6.20 C ATOM 141 CG1 VAL A 23 35.035 13.445 −19.373 1.00 6.20 C ATOM 142 CG2 VAL A 23 35.621 11.158 −18.621 1.00 6.20 C ATOM 143 N ASN A 24 32.063 13.992 −17.660 1.00 12.34 N ATOM 144 CA ASN A 24 31.500 15.306 −17.856 1.00 12.34 C ATOM 145 C ASN A 24 31.763 15.802 −19.278 1.00 12.34 C ATOM 146 O ASN A 24 32.847 15.611 −19.827 1.00 12.34 O ATOM 147 CB ASN A 24 32.159 16.225 −16.834 1.00 12.34 C ATOM 148 CG ASN A 24 31.539 17.601 −16.776 1.00 12.34 C ATOM 149 OD1 ASN A 24 31.598 18.362 −17.739 1.00 12.34 O ATOM 150 ND2 ASN A 24 30.977 17.947 −15.619 1.00 12.34 N ATOM 151 N ALA A 25 30.759 16.422 −19.885 1.00 27.74 N ATOM 152 CA ALA A 25 30.915 16.979 −21.222 1.00 27.74 C ATOM 153 C ALA A 25 32.028 18.022 −21.223 1.00 27.74 C ATOM 154 O ALA A 25 32.465 18.485 −22.276 1.00 27.74 O ATOM 155 CB ALA A 25 29.603 17.589 −21.707 1.00 27.74 C ATOM 156 N ASP A 26 32.476 18.388 −20.028 1.00 4.55 N ATOM 157 CA ASP A 26 33.552 19.352 −19.868 1.00 4.55 C ATOM 158 C ASP A 26 34.844 18.687 −19.410 1.00 4.55 C ATOM 159 O ASP A 26 35.682 19.320 −18.776 1.00 4.55 O ATOM 160 CB ASP A 26 33.144 20.440 −18.888 1.00 4.55 C ATOM 161 CG ASP A 26 32.018 21.283 −19.416 1.00 4.55 C ATOM 162 OD1 ASP A 26 31.853 21.319 −20.657 1.00 4.55 O ATOM 163 OD2 ASP A 26 31.300 21.906 −18.600 1.00 4.55 O ATOM 164 N GLY A 27 34.994 17.408 −19.744 1.00 34.53 N ATOM 165 CA GLY A 27 36.201 16.664 −19.440 1.00 34.53 C ATOM 166 C GLY A 27 36.470 16.496 −17.957 1.00 34.53 C ATOM 167 O GLY A 27 37.603 16.671 −17.502 1.00 34.53 O ATOM 168 N GLN A 28 35.433 16.152 −17.201 1.00 24.27 N ATOM 169 CA GLN A 28 35.573 15.964 −15.763 1.00 24.27 C ATOM 170 C GLN A 28 35.105 14.587 −15.337 1.00 24.27 C ATOM 171 O GLN A 28 33.998 14.165 −15.664 1.00 24.27 O ATOM 172 CB GLN A 28 34.799 17.031 −14.994 1.00 24.27 C ATOM 173 CG GLN A 28 35.509 18.356 −14.899 1.00 24.27 C ATOM 174 CD GLN A 28 34.549 19.507 −14.680 1.00 24.27 C ATOM 175 OE1 GLN A 28 33.330 19.354 −14.813 1.00 24.27 O ATOM 176 NE2 GLN A 28 35.095 20.673 −14.347 1.00 24.27 N ATOM 177 N TYR A 29 35.960 13.887 −14.604 1.00 21.92 N ATOM 178 CA TYR A 29 35.623 12.570 −14.094 1.00 21.92 C ATOM 179 C TYR A 29 34.580 12.673 −12.986 1.00 21.92 C ATOM 180 O TYR A 29 34.760 13.421 −12.023 1.00 21.92 O ATOM 181 CB TYR A 29 36.882 11.867 −13.589 1.00 21.92 C ATOM 182 CG TYR A 29 37.648 11.151 −14.680 1.00 21.92 C ATOM 183 CD1 TYR A 29 38.688 11.776 −15.369 1.00 21.92 C ATOM 184 CD2 TYR A 29 37.321 9.853 −15.036 1.00 21.92 C ATOM 185 CE1 TYR A 29 39.380 11.117 −16.379 1.00 21.92 C ATOM 186 CE2 TYR A 29 38.006 9.188 −16.034 1.00 21.92 C ATOM 187 CZ TYR A 29 39.033 9.818 −16.702 1.00 21.92 C ATOM 188 OH TYR A 29 39.697 9.123 −17.689 1.00 21.92 O ATOM 189 N LEU A 30 33.482 11.935 −13.133 1.00 15.05 N ATOM 190 CA LEU A 30 32.438 11.901 −12.111 1.00 15.05 C ATOM 191 C LEU A 30 32.374 10.536 −11.457 1.00 15.05 C ATOM 192 O LEU A 30 32.311 9.519 −12.149 1.00 15.05 O ATOM 193 CB LEU A 30 31.079 12.241 −12.715 1.00 15.05 C ATOM 194 CG LEU A 30 30.974 13.643 −13.311 1.00 15.05 C ATOM 195 CD1 LEU A 30 29.864 13.689 −14.331 1.00 15.05 C ATOM 196 CD2 LEU A 30 30.762 14.693 −12.228 1.00 15.05 C ATOM 197 N PHE A 31 32.388 10.511 −10.126 1.00 20.95 N ATOM 198 CA PHE A 31 32.362 9.248 −9.392 1.00 20.95 C ATOM 199 C PHE A 31 30.959 8.683 −9.337 1.00 20.95 C ATOM 200 O PHE A 31 30.029 9.369 −8.902 1.00 20.95 O ATOM 201 CB PHE A 31 32.882 9.427 −7.971 1.00 20.95 C ATOM 202 CG PHE A 31 32.633 8.241 −7.086 1.00 20.95 C ATOM 203 CD1 PHE A 31 33.434 7.121 −7.169 1.00 20.95 C ATOM 204 CD2 PHE A 31 31.603 8.248 −6.170 1.00 20.95 C ATOM 205 CE1 PHE A 31 33.209 6.035 −6.358 1.00 20.95 C ATOM 206 CE2 PHE A 31 31.380 7.163 −5.361 1.00 20.95 C ATOM 207 CZ PHE A 31 32.183 6.057 −5.457 1.00 20.95 C ATOM 208 N CYS A 32 30.810 7.434 −9.772 1.00 9.72 N ATOM 209 CA CYS A 32 29.491 6.799 −9.823 1.00 9.72 C ATOM 210 C CYS A 32 29.248 5.755 −8.733 1.00 9.72 C ATOM 211 O CYS A 32 30.177 5.225 −8.111 1.00 9.72 O ATOM 212 CB CYS A 32 29.232 6.182 −11.196 1.00 9.72 C ATOM 213 SG CYS A 32 29.264 7.361 −12.514 1.00 9.72 S ATOM 214 N ARG A 33 27.978 5.453 −8.530 1.00 30.78 N ATOM 215 CA ARG A 33 27.573 4.574 −7.464 1.00 30.78 C ATOM 216 C ARG A 33 26.331 3.832 −7.946 1.00 30.78 C ATOM 217 O ARG A 33 25.457 4.443 −8.564 1.00 30.78 O ATOM 218 CB ARG A 33 27.260 5.429 −6.241 1.00 30.78 C ATOM 219 CG ARG A 33 27.366 4.732 −4.909 1.00 30.78 C ATOM 220 CD ARG A 33 27.155 5.735 −3.792 1.00 30.78 C ATOM 221 NE ARG A 33 28.391 6.411 −3.439 1.00 30.78 N ATOM 222 CZ ARG A 33 29.078 6.147 −2.337 1.00 30.78 C ATOM 223 NH1 ARG A 33 28.628 5.234 −1.491 1.00 30.78 N ATOM 224 NH2 ARG A 33 30.201 6.801 −2.074 1.00 30.78 N ATOM 225 N TYR A 34 26.262 2.523 −7.691 1.00 5.08 N ATOM 226 CA TYR A 34 25.136 1.707 −8.157 1.00 5.08 C ATOM 227 C TYR A 34 24.707 0.660 −7.129 1.00 5.08 C ATOM 228 O TYR A 34 25.534 0.086 −6.436 1.00 5.08 O ATOM 229 CB TYR A 34 25.508 1.005 −9.458 1.00 5.08 C ATOM 230 CG TYR A 34 26.105 1.914 −10.497 1.00 5.08 C ATOM 231 CD1 TYR A 34 25.340 2.398 −11.542 1.00 5.08 C ATOM 232 CD2 TYR A 34 27.438 2.285 −10.439 1.00 5.08 C ATOM 233 CE1 TYR A 34 25.878 3.234 −12.503 1.00 5.08 C ATOM 234 CE2 TYR A 34 27.989 3.124 −11.399 1.00 5.08 C ATOM 235 CZ TYR A 34 27.197 3.594 −12.427 1.00 5.08 C ATOM 236 OH TYR A 34 27.727 4.422 −13.381 1.00 5.08 O ATOM 237 N TRP A 35 23.409 0.412 −7.027 1.00 13.62 N ATOM 238 CA TRP A 35 22.908 −0.682 −6.211 1.00 13.62 C ATOM 239 C TRP A 35 21.909 −1.451 −7.052 1.00 13.62 C ATOM 240 O TRP A 35 20.827 −0.943 −7.339 1.00 13.62 O ATOM 241 CB TRP A 35 22.187 −0.164 −4.975 1.00 13.62 C ATOM 242 CG TRP A 35 22.914 0.872 −4.178 1.00 13.62 C ATOM 243 CD1 TRP A 35 23.398 0.732 −2.917 1.00 13.62 C ATOM 244 CD2 TRP A 35 23.200 2.221 −4.567 1.00 13.62 C ATOM 245 NE1 TRP A 35 23.983 1.902 −2.500 1.00 13.62 N ATOM 246 CE2 TRP A 35 23.870 2.830 −3.494 1.00 13.62 C ATOM 247 CE3 TRP A 35 22.963 2.965 −5.721 1.00 13.62 C ATOM 248 CZ2 TRP A 35 24.306 4.139 −3.544 1.00 13.62 C ATOM 249 CZ3 TRP A 35 23.398 4.264 −5.767 1.00 13.62 C ATOM 250 CH2 TRP A 35 24.062 4.839 −4.689 1.00 13.62 C ATOM 251 N ALA A 36 22.258 −2.672 −7.449 1.00 16.85 N ATOM 252 CA ALA A 36 21.387 −3.454 −8.323 1.00 16.85 C ATOM 253 C ALA A 36 21.012 −4.817 −7.747 1.00 16.85 C ATOM 254 CB ALA A 36 22.023 −3.606 −9.694 1.00 16.85 C ATOM 255 O ALA A 36 21.844 −5.497 −7.153 1.00 16.85 O ATOM 256 N PRO A 37 19.748 −5.214 −7.926 1.00 35.26 N ATOM 257 CA PRO A 37 19.210 −6.480 −7.428 1.00 35.26 C ATOM 258 C PRO A 37 19.801 −7.650 −8.202 1.00 35.26 C ATOM 259 O PRO A 37 20.378 −7.444 −9.277 1.00 35.26 O ATOM 260 CB PRO A 37 17.718 −6.359 −7.746 1.00 35.26 C ATOM 261 CG PRO A 37 17.672 −5.434 −8.916 1.00 35.26 C ATOM 262 CD PRO A 37 18.706 −4.408 −8.581 1.00 35.26 C ATOM 263 N THR A 38 19.659 −8.859 −7.666 1.00 55.18 N ATOM 264 CA THR A 38 20.148 −10.051 −8.342 1.00 55.18 C ATOM 265 C THR A 38 19.285 −10.353 −9.552 1.00 55.18 C ATOM 266 O THR A 38 19.790 −10.721 −10.611 1.00 55.18 O ATOM 267 CB THR A 38 20.141 −11.274 −7.415 1.00 55.18 C ATOM 268 OG1 THR A 38 18.801 −11.550 −6.987 1.00 55.18 O ATOM 269 CG2 THR A 38 21.020 −11.024 −6.205 1.00 55.18 C ATOM 270 N GLY A 39 17.977 −10.183 −9.390 1.00 48.70 N ATOM 271 CA GLY A 39 17.027 −10.476 −10.449 1.00 48.70 C ATOM 272 C GLY A 39 17.044 −9.495 −11.611 1.00 48.70 C ATOM 273 O GLY A 39 18.074 −8.896 −11.922 1.00 48.70 O ATOM 274 N THR A 40 15.893 −9.337 −12.258 1.00 53.42 N ATOM 275 CA THR A 40 15.767 −8.427 −13.385 1.00 53.42 C ATOM 276 C THR A 40 15.195 −7.092 −12.934 1.00 53.42 C ATOM 277 O THR A 40 14.060 −7.031 −12.451 1.00 53.42 O ATOM 278 CB THR A 40 14.843 −8.994 −14.469 1.00 53.42 C ATOM 279 OG1 THR A 40 15.335 −10.267 −14.909 1.00 53.42 O ATOM 280 CG2 THR A 40 14.770 −8.041 −15.649 1.00 53.42 C ATOM 281 N PRO A 41 15.984 −6.015 −13.095 1.00 47.70 N ATOM 282 CA PRO A 41 15.594 −4.652 −12.719 1.00 47.70 C ATOM 283 C PRO A 41 14.183 −4.298 −13.178 1.00 47.70 C ATOM 284 O PRO A 41 13.933 −4.241 −14.380 1.00 47.70 O ATOM 285 CB PRO A 41 16.615 −3.789 −13.461 1.00 47.70 C ATOM 286 CG PRO A 41 17.831 −4.652 −13.541 1.00 47.70 C ATOM 287 CD PRO A 41 17.339 −6.063 −13.678 1.00 47.70 C ATOM 288 N LYS A 42 13.277 −4.077 −12.229 1.00 12.15 N ATOM 289 CA LYS A 42 11.933 −3.598 −12.541 1.00 12.15 C ATOM 290 C LYS A 42 12.017 −2.229 −13.192 1.00 12.15 C ATOM 291 O LYS A 42 11.383 −1.968 −14.208 1.00 12.15 O ATOM 292 CB LYS A 42 11.080 −3.484 −11.277 1.00 12.15 C ATOM 293 CG LYS A 42 10.318 −4.740 −10.861 1.00 12.15 C ATOM 294 CD LYS A 42 9.094 −4.339 −10.030 1.00 12.15 C ATOM 295 CE LYS A 42 8.570 −5.465 −9.155 1.00 12.15 C ATOM 296 NZ LYS A 42 7.194 −5.186 −8.666 1.00 12.15 N ATOM 297 N ALA A 43 12.798 −1.346 −12.588 1.00 10.76 N ATOM 298 CA ALA A 43 13.043 −0.041 −13.174 1.00 10.76 C ATOM 299 C ALA A 43 14.346 0.540 −12.650 1.00 10.76 C ATOM 300 O ALA A 43 15.079 −0.114 −11.892 1.00 10.76 O ATOM 301 CB ALA A 43 11.889 0.891 −12.897 1.00 10.76 C ATOM 302 N LEU A 44 14.626 1.771 −13.068 1.00 37.59 N ATOM 303 CA LEU A 44 15.843 2.479 −12.689 1.00 37.59 C ATOM 304 C LEU A 44 15.491 3.726 −11.887 1.00 37.59 C ATOM 305 O LEU A 44 14.382 4.243 −11.999 1.00 37.59 O ATOM 306 CB LEU A 44 16.607 2.887 −13.946 1.00 37.59 C ATOM 307 CG LEU A 44 16.866 1.764 −14.950 1.00 37.59 C ATOM 308 CD1 LEU A 44 16.987 2.289 −16.380 1.00 37.59 C ATOM 309 CD2 LEU A 44 18.109 0.998 −14.540 1.00 37.59 C ATOM 310 N ILE A 45 16.428 4.211 −11.077 1.00 4.93 N ATOM 311 CA ILE A 45 16.218 5.466 −10.358 1.00 4.93 C ATOM 312 C ILE A 45 17.514 6.174 −9.987 1.00 4.93 C ATOM 313 O ILE A 45 18.407 5.595 −9.363 1.00 4.93 O ATOM 314 CB ILE A 45 15.366 5.261 −9.099 1.00 4.93 C ATOM 315 CG1 ILE A 45 15.194 6.588 −8.348 1.00 4.93 C ATOM 316 CG2 ILE A 45 15.976 4.163 −8.220 1.00 4.93 C ATOM 317 CD1 ILE A 45 14.154 6.549 −7.265 1.00 4.93 C ATOM 318 N PHE A 46 17.600 7.442 −10.370 1.00 6.06 N ATOM 319 CA PHE A 46 18.805 8.225 −10.147 1.00 6.06 C ATOM 320 C PHE A 46 18.673 9.098 −8.916 1.00 6.06 C ATOM 321 O PHE A 46 17.647 9.723 −8.695 1.00 6.06 O ATOM 322 CB PHE A 46 19.101 9.095 −11.358 1.00 6.06 C ATOM 323 CG PHE A 46 20.335 9.900 −11.217 1.00 6.06 C ATOM 324 CD1 PHE A 46 20.294 11.140 −10.598 1.00 6.06 C ATOM 325 CD2 PHE A 46 21.543 9.420 −11.688 1.00 6.06 C ATOM 326 CE1 PHE A 46 21.438 11.905 −10.456 1.00 6.06 C ATOM 327 CE2 PHE A 46 22.699 10.169 −11.550 1.00 6.06 C ATOM 328 CZ PHE A 46 22.646 11.421 −10.932 1.00 6.06 C ATOM 329 N VAL A 47 19.730 9.148 −8.120 1.00 7.98 N ATOM 330 CA VAL A 47 19.668 9.792 −6.815 1.00 7.98 C ATOM 331 C VAL A 47 20.508 11.049 −6.782 1.00 7.98 C ATOM 332 O VAL A 47 21.708 11.000 −6.978 1.00 7.98 O ATOM 333 CB VAL A 47 20.135 8.829 −5.700 1.00 7.98 C ATOM 334 CG1 VAL A 47 20.175 9.530 −4.363 1.00 7.98 C ATOM 335 CG2 VAL A 47 19.222 7.611 −5.635 1.00 7.98 C ATOM 336 N SER A 48 19.871 12.178 −6.519 1.00 5.13 N ATOM 337 CA SER A 48 20.566 13.445 −6.585 1.00 5.13 C ATOM 338 C SER A 48 20.856 14.014 −5.205 1.00 5.13 C ATOM 339 O SER A 48 19.970 14.555 −4.542 1.00 5.13 O ATOM 340 CB SER A 48 19.771 14.444 −7.428 1.00 5.13 C ATOM 341 OG SER A 48 20.495 15.653 −7.596 1.00 5.13 O ATOM 342 N HIS A 49 22.109 13.893 −4.781 1.00 7.76 N ATOM 343 CA HIS A 49 22.549 14.463 −3.514 1.00 7.76 C ATOM 344 C HIS A 49 22.540 15.989 −3.580 1.00 7.76 C ATOM 345 O HIS A 49 22.619 16.573 −4.663 1.00 7.76 O ATOM 346 CB HIS A 49 23.939 13.930 −3.118 1.00 7.76 C ATOM 347 CG HIS A 49 25.081 14.514 −3.901 1.00 7.76 C ATOM 348 ND1 HIS A 49 25.428 15.848 −3.839 1.00 7.76 N ATOM 349 CD2 HIS A 49 25.984 13.932 −4.725 1.00 7.76 C ATOM 350 CE1 HIS A 49 26.480 16.064 −4.606 1.00 7.76 C ATOM 351 NE2 HIS A 49 26.835 14.919 −5.155 1.00 7.76 N ATOM 352 N GLY A 50 22.452 16.629 −2.419 1.00 4.73 N ATOM 353 CA GLY A 50 22.313 18.069 −2.370 1.00 4.73 C ATOM 354 C GLY A 50 23.640 18.774 −2.317 1.00 4.73 C ATOM 355 O GLY A 50 24.685 18.156 −2.500 1.00 4.73 O ATOM 356 N ALA A 51 23.588 20.078 −2.068 1.00 59.32 N ATOM 357 CA ALA A 51 24.789 20.893 −1.945 1.00 59.32 C ATOM 358 C ALA A 51 25.621 20.425 −0.757 1.00 59.32 C ATOM 359 O ALA A 51 25.115 19.751 0.136 1.00 59.32 O ATOM 360 CB ALA A 51 24.426 22.362 −1.807 1.00 59.32 C ATOM 361 N GLY A 52 26.904 20.766 −0.761 1.00 15.52 N ATOM 362 CA GLY A 52 27.791 20.379 0.312 1.00 15.52 C ATOM 363 C GLY A 52 28.056 18.891 0.396 1.00 15.52 C ATOM 364 O GLY A 52 29.168 18.487 0.708 1.00 15.52 O ATOM 365 N GLU A 53 27.048 18.070 0.125 1.00 6.06 N ATOM 366 CA GLU A 53 27.149 16.636 0.401 1.00 6.06 C ATOM 367 C GLU A 53 27.530 15.804 −0.816 1.00 6.06 C ATOM 368 O GLU A 53 28.194 16.292 −1.729 1.00 6.06 O ATOM 369 CB GLU A 53 25.856 16.103 1.032 1.00 6.06 C ATOM 370 CG GLU A 53 24.593 16.471 0.283 1.00 6.06 C ATOM 371 CD GLU A 53 23.409 15.615 0.673 1.00 6.06 C ATOM 372 OE1 GLU A 53 23.524 14.801 1.620 1.00 6.06 O ATOM 373 OE2 GLU A 53 22.360 15.762 0.018 1.00 6.06 O ATOM 374 N HIS A 54 27.110 14.544 −0.822 1.00 18.52 N ATOM 375 CA HIS A 54 27.473 13.652 −1.910 1.00 18.52 C ATOM 376 C HIS A 54 26.583 12.428 −1.931 1.00 18.52 C ATOM 377 O HIS A 54 25.635 12.329 −1.153 1.00 18.52 O ATOM 378 CB HIS A 54 28.921 13.220 −1.761 1.00 18.52 C ATOM 379 CG HIS A 54 29.204 12.559 −0.454 1.00 18.52 C ATOM 380 ND1 HIS A 54 29.459 11.210 −0.343 1.00 18.52 N ATOM 381 CD2 HIS A 54 29.248 13.058 0.803 1.00 18.52 C ATOM 382 CE1 HIS A 54 29.663 10.907 0.926 1.00 18.52 C ATOM 383 NE2 HIS A 54 29.541 12.012 1.641 1.00 18.52 N ATOM 384 N SER A 55 26.912 11.498 −2.826 1.00 7.88 N ATOM 385 CA SER A 55 26.124 10.287 −3.034 1.00 7.88 C ATOM 386 C SER A 55 26.281 9.266 −1.908 1.00 7.88 C ATOM 387 O SER A 55 25.443 8.389 −1.728 1.00 7.88 O ATOM 388 CB SER A 55 26.482 9.638 −4.375 1.00 7.88 C ATOM 389 OG SER A 55 27.771 9.055 −4.341 1.00 7.88 O ATOM 390 N GLY A 56 27.363 9.379 −1.153 1.00 16.43 N ATOM 391 CA GLY A 56 27.616 8.450 −0.073 1.00 16.43 C ATOM 392 C GLY A 56 26.453 8.327 0.882 1.00 16.43 C ATOM 393 O GLY A 56 26.193 7.248 1.402 1.00 16.43 O ATOM 394 N ARG A 57 25.733 9.425 1.083 1.00 9.70 N ATOM 395 CA ARG A 57 24.768 9.556 2.172 1.00 9.70 C ATOM 396 C ARG A 57 23.385 8.997 1.873 1.00 9.70 C ATOM 397 O ARG A 57 22.518 8.963 2.740 1.00 9.70 O ATOM 398 CB ARG A 57 24.626 11.026 2.555 1.00 9.70 C ATOM 399 CG ARG A 57 25.941 11.761 2.686 1.00 9.70 C ATOM 400 CD ARG A 57 25.724 13.253 2.776 1.00 9.70 C ATOM 401 NE ARG A 57 24.784 13.621 3.833 1.00 9.70 N ATOM 402 CZ ARG A 57 25.025 13.458 5.129 1.00 9.70 C ATOM 403 NH1 ARG A 57 26.175 12.919 5.525 1.00 9.70 N ATOM 404 NH2 ARG A 57 24.121 13.825 6.030 1.00 9.70 N ATOM 405 N TYR A 58 23.168 8.562 0.644 1.00 17.54 N ATOM 406 CA TYR A 58 21.880 7.991 0.280 1.00 17.54 C ATOM 407 C TYR A 58 21.941 6.472 0.219 1.00 17.54 C ATOM 408 O TYR A 58 21.205 5.835 −0.528 1.00 17.54 O ATOM 409 CB TYR A 58 21.416 8.578 −1.047 1.00 17.54 C ATOM 410 CG TYR A 58 21.191 10.063 −0.958 1.00 17.54 C ATOM 411 CD1 TYR A 58 22.258 10.943 −0.970 1.00 17.54 C ATOM 412 CD2 TYR A 58 19.908 10.586 −0.843 1.00 17.54 C ATOM 413 CE1 TYR A 58 22.050 12.302 −0.880 1.00 17.54 C ATOM 414 CE2 TYR A 58 19.694 11.938 −0.753 1.00 17.54 C ATOM 415 CZ TYR A 58 20.767 12.792 −0.773 1.00 17.54 C ATOM 416 OH TYR A 58 20.571 14.147 −0.683 1.00 17.54 O ATOM 417 N GLU A 59 22.820 5.898 1.029 1.00 15.15 N ATOM 418 CA GLU A 59 23.050 4.465 1.007 1.00 15.15 C ATOM 419 C GLU A 59 21.829 3.695 1.499 1.00 15.15 C ATOM 420 O GLU A 59 21.367 2.762 0.854 1.00 15.15 O ATOM 421 CB GLU A 59 24.270 4.122 1.855 1.00 15.15 C ATOM 422 CG GLU A 59 24.753 2.698 1.662 1.00 15.15 C ATOM 423 CD GLU A 59 25.516 2.493 0.354 1.00 15.15 C ATOM 424 OE1 GLU A 59 26.044 3.495 −0.195 1.00 15.15 O ATOM 425 OE2 GLU A 59 25.589 1.324 −0.114 1.00 15.15 O ATOM 426 N GLU A 60 21.317 4.106 2.648 1.00 14.24 N ATOM 427 CA GLU A 60 20.154 3.494 3.276 1.00 14.24 C ATOM 428 C GLU A 60 18.913 3.546 2.378 1.00 14.24 C ATOM 429 O GLU A 60 18.125 2.605 2.328 1.00 14.24 O ATOM 430 CB GLU A 60 19.853 4.209 4.601 1.00 14.24 C ATOM 431 CG GLU A 60 21.052 4.958 5.241 1.00 14.24 C ATOM 432 CD GLU A 60 21.425 6.297 4.547 1.00 14.24 C ATOM 433 OE1 GLU A 60 22.571 6.764 4.764 1.00 14.24 O ATOM 434 OE2 GLU A 60 20.593 6.877 3.791 1.00 14.24 O ATOM 435 N LEU A 61 18.733 4.657 1.680 1.00 18.51 N ATOM 436 CA LEU A 61 17.554 4.830 0.838 1.00 18.51 C ATOM 437 C LEU A 61 17.639 3.948 −0.388 1.00 18.51 C ATOM 438 O LEU A 61 16.657 3.331 −0.783 1.00 18.51 O ATOM 439 CB LEU A 61 17.393 6.290 0.405 1.00 18.51 C ATOM 440 CG LEU A 61 16.939 7.259 1.495 1.00 18.51 C ATOM 441 CD1 LEU A 61 18.146 7.850 2.237 1.00 18.51 C ATOM 442 CD2 LEU A 61 16.101 8.340 0.875 1.00 18.51 C ATOM 443 N ALA A 62 18.821 3.899 −0.987 1.00 34.10 N ATOM 444 CA ALA A 62 19.062 3.061 −2.154 1.00 34.10 C ATOM 445 C ALA A 62 18.826 1.595 −1.849 1.00 34.10 C ATOM 446 O ALA A 62 18.156 0.898 −2.604 1.00 34.10 O ATOM 447 CB ALA A 62 20.473 3.255 −2.648 1.00 34.10 C ATOM 448 N ARG A 63 19.392 1.127 −0.747 1.00 15.73 N ATOM 449 CA ARG A 63 19.220 −0.254 −0.338 1.00 15.73 C ATOM 450 C ARG A 63 17.766 −0.679 −0.235 1.00 15.73 C ATOM 451 O ARG A 63 17.455 −1.860 −0.305 1.00 15.73 O ATOM 452 CB ARG A 63 19.934 −0.496 0.974 1.00 15.73 C ATOM 453 CG ARG A 63 21.369 −0.835 0.750 1.00 15.73 C ATOM 454 CD ARG A 63 22.243 −0.316 1.850 1.00 15.73 C ATOM 455 NE ARG A 63 23.623 −0.705 1.607 1.00 15.73 N ATOM 456 CZ ARG A 63 24.628 −0.471 2.443 1.00 15.73 C ATOM 457 NH1 ARG A 63 24.417 0.164 3.592 1.00 15.73 N ATOM 458 NH2 ARG A 63 25.846 −0.876 2.120 1.00 15.73 N ATOM 459 N MET A 64 16.869 0.278 −0.071 1.00 5.66 N ATOM 460 CA MET A 64 15.458 −0.046 −0.021 1.00 5.66 C ATOM 461 C MET A 64 14.828 0.036 −1.400 1.00 5.66 C ATOM 462 O MET A 64 13.893 −0.699 −1.713 1.00 5.66 O ATOM 463 CB MET A 64 14.729 0.863 0.963 1.00 5.66 C ATOM 464 CG MET A 64 13.244 0.938 0.718 1.00 5.66 C ATOM 465 SD MET A 64 12.711 2.487 −0.045 1.00 5.66 S ATOM 466 CE MET A 64 13.046 3.555 1.375 1.00 5.66 C ATOM 467 N LEU A 65 15.325 0.940 −2.228 1.00 4.62 N ATOM 468 CA LEU A 65 14.785 1.044 −3.562 1.00 4.62 C ATOM 469 C LEU A 65 15.282 −0.177 −4.283 1.00 4.62 C ATOM 470 O LEU A 65 14.511 −0.893 −4.909 1.00 4.62 O ATOM 471 CB LEU A 65 15.248 2.327 −4.237 1.00 4.62 C ATOM 472 CG LEU A 65 14.857 3.591 −3.448 1.00 4.62 C ATOM 473 CD1 LEU A 65 15.711 4.789 −3.832 1.00 4.62 C ATOM 474 CD2 LEU A 65 13.376 3.929 −3.587 1.00 4.62 C ATOM 475 N MET A 66 16.575 −0.442 −4.146 1.00 38.26 N ATOM 476 CA MET A 66 17.194 −1.613 −4.757 1.00 38.26 C ATOM 477 C MET A 66 16.544 −2.903 −4.251 1.00 38.26 C ATOM 478 O MET A 66 16.303 −3.834 −5.019 1.00 38.26 O ATOM 479 CB MET A 66 18.706 −1.598 −4.502 1.00 38.26 C ATOM 480 CG MET A 66 19.463 −2.776 −5.075 1.00 38.26 C ATOM 481 SD MET A 66 19.670 −4.041 −3.825 1.00 38.26 S ATOM 482 CE MET A 66 20.669 −3.142 −2.647 1.00 38.26 C ATOM 483 N GLY A 67 16.254 −2.941 −2.956 1.00 22.28 N ATOM 484 CA GLY A 67 15.475 −4.019 −2.384 1.00 22.28 C ATOM 485 C GLY A 67 14.154 −4.135 −3.118 1.00 22.28 C ATOM 486 O GLY A 67 13.670 −5.234 −3.376 1.00 22.28 O ATOM 487 N LEU A 68 13.569 −2.993 −3.466 1.00 23.89 N ATOM 488 CA LEU A 68 12.313 −2.971 −4.217 1.00 23.89 C ATOM 489 C LEU A 68 12.530 −3.490 −5.637 1.00 23.89 C ATOM 490 O LEU A 68 11.670 −3.356 −6.502 1.00 23.89 O ATOM 491 CB LEU A 68 11.717 −1.556 −4.266 1.00 23.89 C ATOM 492 CG LEU A 68 10.913 −0.996 −3.094 1.00 23.89 C ATOM 493 CD1 LEU A 68 9.956 0.032 −3.628 1.00 23.89 C ATOM 494 CD2 LEU A 68 10.137 −2.081 −2.396 1.00 23.89 C ATOM 495 N ASP A 69 13.700 −4.070 −5.867 1.00 40.55 N ATOM 496 CA ASP A 69 14.052 −4.609 −7.172 1.00 40.55 C ATOM 497 C ASP A 69 14.156 −3.500 −8.218 1.00 40.55 C ATOM 498 O ASP A 69 13.700 −3.647 −9.353 1.00 40.55 O ATOM 499 CB ASP A 69 13.073 −5.714 −7.588 1.00 40.55 C ATOM 500 CG ASP A 69 13.197 −6.959 −6.714 1.00 40.55 C ATOM 501 OD1 ASP A 69 12.159 −7.499 −6.277 1.00 40.55 O ATOM 502 OD2 ASP A 69 14.338 −7.390 −6.449 1.00 40.55 O ATOM 503 N LEU A 70 14.764 −2.389 −7.814 1.00 9.32 N ATOM 504 CA LEU A 70 15.110 −1.321 −8.736 1.00 9.32 C ATOM 505 C LEU A 70 16.615 −1.199 −8.810 1.00 9.32 C ATOM 506 O LEU A 70 17.312 −1.447 −7.827 1.00 9.32 O ATOM 507 CB LEU A 70 14.530 0.021 −8.277 1.00 9.32 C ATOM 508 CG LEU A 70 13.134 0.425 −8.758 1.00 9.32 C ATOM 509 CD1 LEU A 70 12.058 −0.490 −8.175 1.00 9.32 C ATOM 510 CD2 LEU A 70 12.870 1.869 −8.404 1.00 9.32 C ATOM 511 N LEU A 71 17.117 −0.817 −9.978 1.00 18.64 N ATOM 512 CA LEU A 71 18.534 −0.562 −10.120 1.00 18.64 C ATOM 513 C LEU A 71 18.771 0.869 −9.721 1.00 18.64 C ATOM 514 O LEU A 71 18.582 1.781 −10.525 1.00 18.64 O ATOM 515 CB LEU A 71 18.988 −0.746 −11.566 1.00 18.64 C ATOM 516 CG LEU A 71 20.504 −0.815 −11.815 1.00 18.64 C ATOM 517 CD1 LEU A 71 20.799 −0.525 −13.266 1.00 18.64 C ATOM 518 CD2 LEU A 71 21.304 0.125 −10.935 1.00 18.64 C ATOM 519 N VAL A 72 19.192 1.079 −8.487 1.00 30.24 N ATOM 520 CA VAL A 72 19.522 2.427 −8.072 1.00 30.24 C ATOM 521 C VAL A 72 20.901 2.812 −8.590 1.00 30.24 C ATOM 522 O VAL A 72 21.863 2.053 −8.484 1.00 30.24 O ATOM 523 CB VAL A 72 19.436 2.593 −6.550 1.00 30.24 C ATOM 524 CG1 VAL A 72 19.793 4.015 −6.159 1.00 30.24 C ATOM 525 CG2 VAL A 72 18.036 2.249 −6.073 1.00 30.24 C ATOM 526 N PHE A 73 20.987 3.988 −9.187 1.00 8.18 N ATOM 527 CA PHE A 73 22.283 4.499 −9.600 1.00 8.18 C ATOM 528 C PHE A 73 22.413 5.991 −9.304 1.00 8.18 C ATOM 529 O PHE A 73 21.414 6.686 −9.062 1.00 8.18 O ATOM 530 CB PHE A 73 22.565 4.186 −11.071 1.00 8.18 C ATOM 531 CG PHE A 73 21.690 4.924 −12.032 1.00 8.18 C ATOM 532 CD1 PHE A 73 20.327 4.673 −12.082 1.00 8.18 C ATOM 533 CD2 PHE A 73 22.237 5.845 −12.910 1.00 8.18 C ATOM 534 CE1 PHE A 73 19.526 5.338 −12.974 1.00 8.18 C ATOM 535 CE2 PHE A 73 21.438 6.515 −13.807 1.00 8.18 C ATOM 536 CZ PHE A 73 20.080 6.261 −13.841 1.00 8.18 C ATOM 537 N ALA A 74 23.653 6.470 −9.320 1.00 6.53 N ATOM 538 CA ALA A 74 23.933 7.823 −8.895 1.00 6.53 C ATOM 539 C ALA A 74 25.404 8.168 −9.086 1.00 6.53 C ATOM 540 O ALA A 74 26.260 7.287 −9.024 1.00 6.53 O ATOM 541 CB ALA A 74 23.542 7.970 −7.434 1.00 6.53 C ATOM 542 N HIS A 75 25.685 9.454 −9.306 1.00 21.44 N ATOM 543 CA HIS A 75 27.054 9.967 −9.290 1.00 21.44 C ATOM 544 C HIS A 75 27.239 11.205 −8.404 1.00 21.44 C ATOM 545 O HIS A 75 26.345 11.598 −7.650 1.00 21.44 O ATOM 546 CB HIS A 75 27.545 10.264 −10.707 1.00 21.44 C ATOM 547 CG HIS A 75 26.725 11.285 −11.434 1.00 21.44 C ATOM 548 ND1 HIS A 75 25.827 10.949 −12.427 1.00 21.44 N ATOM 549 CD2 HIS A 75 26.672 12.634 −11.317 1.00 21.44 C ATOM 550 CE1 HIS A 75 25.256 12.050 −12.889 1.00 21.44 C ATOM 551 NE2 HIS A 75 25.752 13.086 −12.234 1.00 21.44 N ATOM 552 N ASP A 76 28.418 11.814 −8.508 1.00 8.80 N ATOM 553 CA ASP A 76 28.756 12.979 −7.699 1.00 8.80 C ATOM 554 C ASP A 76 28.922 14.297 −8.456 1.00 8.80 C ATOM 555 O ASP A 76 29.929 14.536 −9.118 1.00 8.80 O ATOM 556 CB ASP A 76 30.004 12.710 −6.880 1.00 8.80 C ATOM 557 CG ASP A 76 29.682 12.230 −5.506 1.00 8.80 C ATOM 558 OD1 ASP A 76 28.518 11.833 −5.283 1.00 8.80 O ATOM 559 OD2 ASP A 76 30.586 12.264 −4.650 1.00 8.80 O ATOM 560 N HIS A 77 27.924 15.158 −8.313 1.00 15.08 N ATOM 561 CA HIS A 77 27.953 16.486 −8.887 1.00 15.08 C ATOM 562 C HIS A 77 29.352 17.093 −8.909 1.00 15.08 C ATOM 563 O HIS A 77 30.082 17.029 −7.929 1.00 15.08 O ATOM 564 CB HIS A 77 27.004 17.394 −8.113 1.00 15.08 C ATOM 565 CG HIS A 77 25.603 16.876 −8.033 1.00 15.08 C ATOM 566 ND1 HIS A 77 24.874 16.528 −9.149 1.00 15.08 N ATOM 567 CD2 HIS A 77 24.788 16.666 −6.971 1.00 15.08 C ATOM 568 CE1 HIS A 77 23.674 16.116 −8.778 1.00 15.08 C ATOM 569 NE2 HIS A 77 23.595 16.192 −7.460 1.00 15.08 N ATOM 570 N VAL A 78 29.717 17.681 −10.043 1.00 19.63 N ATOM 571 CA VAL A 78 31.020 18.312 −10.208 1.00 19.63 C ATOM 572 C VAL A 78 31.304 19.259 −9.049 1.00 19.63 C ATOM 573 CB VAL A 78 31.096 19.084 −11.542 1.00 19.63 C ATOM 574 CG1 VAL A 78 30.191 20.301 −11.504 1.00 19.63 C ATOM 575 CG2 VAL A 78 32.524 19.490 −11.844 1.00 19.63 C ATOM 576 O VAL A 78 30.444 20.035 −8.650 1.00 19.63 O ATOM 577 N GLY A 79 32.513 19.189 −8.505 1.00 8.56 N ATOM 578 CA GLY A 79 32.867 20.020 −7.373 1.00 8.56 C ATOM 579 C GLY A 79 32.294 19.428 −6.112 1.00 8.56 C ATOM 580 O GLY A 79 32.165 20.100 −5.094 1.00 8.56 O ATOM 581 N HIS A 80 31.941 18.152 −6.191 1.00 7.88 N ATOM 582 CA HIS A 80 31.410 17.427 −5.043 1.00 7.88 C ATOM 583 C HIS A 80 32.022 16.043 −4.923 1.00 7.88 C ATOM 584 O HIS A 80 32.382 15.423 −5.924 1.00 7.88 O ATOM 585 CB HIS A 80 29.893 17.281 −5.146 1.00 7.88 C ATOM 586 CG HIS A 80 29.145 18.526 −4.807 1.00 7.88 C ATOM 587 ND1 HIS A 80 28.896 19.519 −5.729 1.00 7.88 N ATOM 588 CD2 HIS A 80 28.600 18.944 −3.642 1.00 7.88 C ATOM 589 CE1 HIS A 80 28.224 20.494 −5.146 1.00 7.88 C ATOM 590 NE2 HIS A 80 28.034 20.171 −3.880 1.00 7.88 N ATOM 591 N GLY A 81 32.118 15.569 −3.683 1.00 44.05 N ATOM 592 CA GLY A 81 32.525 14.211 −3.378 1.00 44.05 C ATOM 593 C GLY A 81 33.720 13.750 −4.176 1.00 44.05 C ATOM 594 O GLY A 81 34.617 14.537 −4.479 1.00 44.05 O ATOM 595 N GLN A 82 33.721 12.472 −4.533 1.00 7.70 N ATOM 596 CA GLN A 82 34.856 11.863 −5.211 1.00 7.70 C ATOM 597 C GLN A 82 34.949 12.199 −6.695 1.00 7.70 C ATOM 598 O GLN A 82 35.590 11.494 −7.455 1.00 7.70 O ATOM 599 CB GLN A 82 34.809 10.354 −5.022 1.00 7.70 C ATOM 600 CG GLN A 82 35.252 9.903 −3.652 1.00 7.70 C ATOM 601 CD GLN A 82 34.678 8.566 −3.302 1.00 7.70 C ATOM 602 OE1 GLN A 82 33.515 8.464 −2.914 1.00 7.70 O ATOM 603 NE2 GLN A 82 35.481 7.522 −3.450 1.00 7.70 N ATOM 604 N SER A 83 34.313 13.284 −7.107 1.00 23.63 N ATOM 605 CA SER A 83 34.353 13.689 −8.499 1.00 23.63 C ATOM 606 C SER A 83 35.204 14.941 −8.651 1.00 23.63 C ATOM 607 O SER A 83 35.415 15.689 −7.693 1.00 23.63 O ATOM 608 CB SER A 83 32.938 13.908 −9.028 1.00 23.63 C ATOM 609 OG SER A 83 32.234 12.675 −9.054 1.00 23.63 O ATOM 610 N GLU A 84 35.704 15.156 −9.859 1.00 18.54 N ATOM 611 CA GLU A 84 36.636 16.243 −10.104 1.00 18.54 C ATOM 612 C GLU A 84 35.910 17.561 −10.097 1.00 18.54 C ATOM 613 O GLU A 84 34.761 17.625 −10.500 1.00 18.54 O ATOM 614 CB GLU A 84 37.357 16.035 −11.437 1.00 18.54 C ATOM 615 CG GLU A 84 38.278 14.826 −11.448 1.00 18.54 C ATOM 616 CD GLU A 84 39.087 14.727 −12.718 1.00 18.54 C ATOM 617 OE1 GLU A 84 38.481 14.792 −13.811 1.00 18.54 O ATOM 618 OE2 GLU A 84 40.328 14.581 −12.618 1.00 18.54 O ATOM 619 N GLY A 85 36.573 18.610 −9.626 1.00 7.13 N ATOM 620 CA GLY A 85 35.976 19.928 −9.630 1.00 7.13 C ATOM 621 C GLY A 85 36.196 20.712 −8.353 1.00 7.13 C ATOM 622 O GLY A 85 36.072 20.186 −7.240 1.00 7.13 O ATOM 623 N GLU A 86 36.522 21.993 −8.525 1.00 20.60 N ATOM 624 CA GLU A 86 36.740 22.899 −7.405 1.00 20.60 C ATOM 625 C GLU A 86 35.507 22.883 −6.519 1.00 20.60 C ATOM 626 O GLU A 86 34.395 23.154 −6.978 1.00 20.60 O ATOM 627 CB GLU A 86 37.043 24.310 −7.908 1.00 20.60 C ATOM 628 CG GLU A 86 37.597 25.252 −6.845 1.00 20.60 C ATOM 629 CD GLU A 86 37.863 26.665 −7.372 1.00 20.60 C ATOM 630 OE1 GLU A 86 38.053 26.836 −8.598 1.00 20.60 O ATOM 631 OE2 GLU A 86 37.883 27.608 −6.553 1.00 20.60 O ATOM 632 N ARG A 87 35.709 22.533 −5.255 1.00 21.00 N ATOM 633 CA ARG A 87 34.601 22.289 −4.345 1.00 21.00 C ATOM 634 C ARG A 87 33.521 23.362 −4.450 1.00 21.00 C ATOM 635 O ARG A 87 33.803 24.551 −4.302 1.00 21.00 O ATOM 636 CB ARG A 87 35.091 22.182 −2.897 1.00 21.00 C ATOM 637 CG ARG A 87 36.043 21.022 −2.605 1.00 21.00 C ATOM 638 CD ARG A 87 35.457 19.664 −2.948 1.00 21.00 C ATOM 639 NE ARG A 87 35.579 19.363 −4.374 1.00 21.00 N ATOM 640 CZ ARG A 87 35.629 18.131 −4.874 1.00 21.00 C ATOM 641 NH1 ARG A 87 35.579 17.079 −4.064 1.00 21.00 N ATOM 642 NH2 ARG A 87 35.739 17.945 −6.182 1.00 21.00 N ATOM 643 N MET A 88 32.289 22.930 −4.718 1.00 5.33 N ATOM 644 CA MET A 88 31.123 23.809 −4.660 1.00 5.33 C ATOM 645 C MET A 88 31.289 25.074 −5.487 1.00 5.33 C ATOM 646 O MET A 88 31.089 26.188 −4.989 1.00 5.33 O ATOM 647 CB MET A 88 30.795 24.175 −3.209 1.00 5.33 C ATOM 648 CG MET A 88 30.759 22.985 −2.287 1.00 5.33 C ATOM 649 SD MET A 88 30.201 23.401 −0.643 1.00 5.33 S ATOM 650 CE MET A 88 28.456 23.586 −0.975 1.00 5.33 C ATOM 651 N VAL A 89 31.687 24.888 −6.741 1.00 33.60 N ATOM 652 CA VAL A 89 31.616 25.937 −7.749 1.00 33.60 C ATOM 653 C VAL A 89 31.383 25.273 −9.094 1.00 33.60 C ATOM 654 O VAL A 89 31.925 24.194 −9.360 1.00 33.60 O ATOM 655 CB VAL A 89 32.884 26.806 −7.816 1.00 33.60 C ATOM 656 CG1 VAL A 89 33.056 27.613 −6.534 1.00 33.60 C ATOM 657 CG2 VAL A 89 34.091 25.948 −8.092 1.00 33.60 C ATOM 658 N VAL A 90 30.570 25.926 −9.926 1.00 5.75 N ATOM 659 CA VAL A 90 30.126 25.361 −11.193 1.00 5.75 C ATOM 660 C VAL A 90 30.074 26.427 −12.290 1.00 5.75 C ATOM 661 O VAL A 90 29.648 27.545 −12.050 1.00 5.75 O ATOM 662 CB VAL A 90 28.741 24.728 −11.029 1.00 5.75 C ATOM 663 CG1 VAL A 90 27.713 25.802 −10.824 1.00 5.75 C ATOM 664 CG2 VAL A 90 28.394 23.872 −12.223 1.00 5.75 C ATOM 665 N SER A 91 30.529 26.074 −13.488 1.00 21.10 N ATOM 666 CA SER A 91 30.472 26.968 −14.639 1.00 21.10 C ATOM 667 C SER A 91 29.083 27.549 −14.788 1.00 21.10 C ATOM 668 O SER A 91 28.916 28.761 −14.901 1.00 21.10 O ATOM 669 CB SER A 91 30.852 26.214 −15.917 1.00 21.10 C ATOM 670 OG SER A 91 30.320 24.896 −15.942 1.00 21.10 O ATOM 671 N ASP A 92 28.094 26.661 −14.812 1.00 16.56 N ATOM 672 CA ASP A 92 26.688 27.034 −14.776 1.00 16.56 C ATOM 673 C ASP A 92 25.843 25.917 −14.175 1.00 16.56 C ATOM 674 O ASP A 92 26.083 24.741 −14.427 1.00 16.56 O ATOM 675 CB ASP A 92 26.164 27.351 −16.161 1.00 16.56 C ATOM 676 CG ASP A 92 24.678 27.499 −16.168 1.00 16.56 C ATOM 677 OD1 ASP A 92 24.193 28.580 −15.762 1.00 16.56 O ATOM 678 OD2 ASP A 92 24.003 26.521 −16.550 1.00 16.56 O ATOM 679 N PHE A 93 24.832 26.293 −13.401 1.00 6.57 N ATOM 680 CA PHE A 93 24.058 25.328 −12.626 1.00 6.57 C ATOM 681 C PHE A 93 23.656 24.126 −13.443 1.00 6.57 C ATOM 682 O PHE A 93 23.727 23.000 −12.962 1.00 6.57 O ATOM 683 CB PHE A 93 22.819 25.978 −12.024 1.00 6.57 C ATOM 684 CG PHE A 93 22.207 25.184 −10.923 1.00 6.57 C ATOM 685 CD1 PHE A 93 22.852 25.045 −9.711 1.00 6.57 C ATOM 686 CD2 PHE A 93 20.988 24.569 −11.090 1.00 6.57 C ATOM 687 CE1 PHE A 93 22.287 24.303 −8.686 1.00 6.57 C ATOM 688 CE2 PHE A 93 20.419 23.825 −10.064 1.00 6.57 C ATOM 689 CZ PHE A 93 21.068 23.697 −8.865 1.00 6.57 C ATOM 690 N HIS A 94 23.250 24.363 −14.686 1.00 22.59 N ATOM 691 CA HIS A 94 22.778 23.282 −15.544 1.00 22.59 C ATOM 692 C HIS A 94 23.778 22.160 −15.649 1.00 22.59 C ATOM 693 O HIS A 94 23.412 21.016 −15.897 1.00 22.59 O ATOM 694 CB HIS A 94 22.479 23.787 −16.946 1.00 22.59 C ATOM 695 CG HIS A 94 22.229 22.694 −17.939 1.00 22.59 C ATOM 696 ND1 HIS A 94 23.248 22.020 −18.577 1.00 22.59 N ATOM 697 CD2 HIS A 94 21.074 22.160 −18.405 1.00 22.59 C ATOM 698 CE1 HIS A 94 22.731 21.117 −19.391 1.00 22.59 C ATOM 699 NE2 HIS A 94 21.414 21.181 −19.305 1.00 22.59 N ATOM 700 N VAL A 95 25.047 22.489 −15.480 1.00 5.04 N ATOM 701 CA VAL A 95 26.069 21.472 −15.583 1.00 5.04 C ATOM 702 C VAL A 95 25.671 20.255 −14.771 1.00 5.04 C ATOM 703 O VAL A 95 25.914 19.122 −15.184 1.00 5.04 O ATOM 704 CB VAL A 95 27.438 21.976 −15.133 1.00 5.04 C ATOM 705 CG1 VAL A 95 28.443 20.855 −15.207 1.00 5.04 C ATOM 706 CG2 VAL A 95 27.884 23.117 −16.023 1.00 5.04 C ATOM 707 N PHE A 96 25.051 20.484 −13.621 1.00 17.84 N ATOM 708 CA PHE A 96 24.616 19.381 −12.790 1.00 17.84 C ATOM 709 C PHE A 96 23.560 18.614 −13.540 1.00 17.84 C ATOM 710 O PHE A 96 23.640 17.394 −13.687 1.00 17.84 O ATOM 711 CB PHE A 96 24.024 19.894 −11.484 1.00 17.84 C ATOM 712 CG PHE A 96 24.988 20.672 −10.653 1.00 17.84 C ATOM 713 CD1 PHE A 96 26.186 20.110 −10.259 1.00 17.84 C ATOM 714 CD2 PHE A 96 24.703 21.964 −10.266 1.00 17.84 C ATOM 715 CE1 PHE A 96 27.080 20.826 −9.494 1.00 17.84 C ATOM 716 CE2 PHE A 96 25.597 22.680 −9.505 1.00 17.84 C ATOM 717 CZ PHE A 96 26.787 22.110 −9.117 1.00 17.84 C ATOM 718 N VAL A 97 22.564 19.352 −14.010 1.00 28.87 N ATOM 719 CA VAL A 97 21.442 18.786 −14.734 1.00 28.87 C ATOM 720 C VAL A 97 21.911 17.891 −15.861 1.00 28.87 C ATOM 721 O VAL A 97 21.704 16.680 −15.835 1.00 28.87 O ATOM 722 CB VAL A 97 20.587 19.888 −15.366 1.00 28.87 C ATOM 723 CG1 VAL A 97 19.554 19.271 −16.292 1.00 28.87 C ATOM 724 CG2 VAL A 97 19.923 20.738 −14.294 1.00 28.87 C ATOM 725 N ARG A 98 22.534 18.509 −16.859 1.00 25.89 N ATOM 726 CA ARG A 98 23.046 17.784 −18.007 1.00 25.89 C ATOM 727 C ARG A 98 23.593 16.434 −17.570 1.00 25.89 C ATOM 728 O ARG A 98 23.136 15.389 −18.019 1.00 25.89 O ATOM 729 CB ARG A 98 24.150 18.592 −18.691 1.00 25.89 C ATOM 730 CG ARG A 98 24.831 17.858 −19.827 1.00 25.89 C ATOM 731 CD ARG A 98 26.103 18.564 −20.245 1.00 25.89 C ATOM 732 NE ARG A 98 27.102 18.569 −19.184 1.00 25.89 N ATOM 733 CZ ARG A 98 28.101 19.441 −19.109 1.00 25.89 C ATOM 734 NH1 ARG A 98 28.231 20.393 −20.028 1.00 25.89 N ATOM 735 NH2 ARG A 98 28.962 19.369 −18.105 1.00 25.89 N ATOM 736 N ASP A 99 24.566 16.483 −16.668 1.00 20.68 N ATOM 737 CA ASP A 99 25.300 15.309 −16.217 1.00 20.68 C ATOM 738 C ASP A 99 24.401 14.178 −15.726 1.00 20.68 C ATOM 739 O ASP A 99 24.703 12.998 −15.931 1.00 20.68 O ATOM 740 CB ASP A 99 26.286 15.704 −15.125 1.00 20.68 C ATOM 741 CG ASP A 99 27.403 16.583 −15.645 1.00 20.68 C ATOM 742 OD1 ASP A 99 27.365 16.965 −16.832 1.00 20.68 O ATOM 743 OD2 ASP A 99 28.327 16.892 −14.867 1.00 20.68 O ATOM 744 N VAL A 100 23.304 14.534 −15.066 1.00 15.02 N ATOM 745 CA VAL A 100 22.323 13.536 −14.680 1.00 15.02 C ATOM 746 C VAL A 100 21.820 12.884 −15.957 1.00 15.02 C ATOM 747 O VAL A 100 21.989 11.682 −16.165 1.00 15.02 O ATOM 748 CB VAL A 100 21.153 14.162 −13.915 1.00 15.02 C ATOM 749 CG1 VAL A 100 20.196 13.086 −13.441 1.00 15.02 C ATOM 750 CG2 VAL A 100 21.666 14.986 −12.735 1.00 15.02 C ATOM 751 N LEU A 101 21.236 13.699 −16.827 1.00 6.38 N ATOM 752 CA LEU A 101 20.779 13.240 −18.136 1.00 6.38 C ATOM 753 C LEU A 101 21.830 12.370 −18.806 1.00 6.38 C ATOM 754 O LEU A 101 21.580 11.220 −19.185 1.00 6.38 O ATOM 755 CB LEU A 101 20.469 14.439 −19.027 1.00 6.38 C ATOM 756 CG LEU A 101 19.134 15.140 −18.764 1.00 6.38 C ATOM 757 CD1 LEU A 101 19.007 16.394 −19.635 1.00 6.38 C ATOM 758 CD2 LEU A 101 17.961 14.177 −18.980 1.00 6.38 C ATOM 759 N GLN A 102 23.007 12.956 −18.962 1.00 22.08 N ATOM 760 CA GLN A 102 24.173 12.243 −19.429 1.00 22.08 C ATOM 761 C GLN A 102 24.145 10.842 −18.822 1.00 22.08 C ATOM 762 O GLN A 102 24.091 9.849 −19.548 1.00 22.08 O ATOM 763 CB GLN A 102 25.426 13.017 −19.009 1.00 22.08 C ATOM 764 CG GLN A 102 26.736 12.646 −19.696 1.00 22.08 C ATOM 765 CD GLN A 102 27.812 13.722 −19.489 1.00 22.08 C ATOM 766 OE1 GLN A 102 27.523 14.931 −19.519 1.00 22.08 O ATOM 767 NE2 GLN A 102 29.051 13.287 −19.270 1.00 22.08 N ATOM 768 N HIS A 103 24.137 10.765 −17.492 1.00 28.40 N ATOM 769 CA HIS A 103 24.214 9.479 −16.802 1.00 28.40 C ATOM 770 C HIS A 103 22.969 8.643 −17.087 1.00 28.40 C ATOM 771 O HIS A 103 23.046 7.430 −17.327 1.00 28.40 O ATOM 772 CB HIS A 103 24.390 9.680 −15.293 1.00 28.40 C ATOM 773 CG HIS A 103 24.820 8.442 −14.560 1.00 28.40 C ATOM 774 ND1 HIS A 103 25.813 8.450 −13.604 1.00 28.40 N ATOM 775 CD2 HIS A 103 24.391 7.159 −14.641 1.00 28.40 C ATOM 776 CE1 HIS A 103 25.977 7.228 −13.128 1.00 28.40 C ATOM 777 NE2 HIS A 103 25.124 6.426 −13.739 1.00 28.40 N ATOM 778 N VAL A 104 21.818 9.302 −17.070 1.00 11.44 N ATOM 779 CA VAL A 104 20.556 8.621 −17.303 1.00 11.44 C ATOM 780 C VAL A 104 20.554 7.928 −18.669 1.00 11.44 C ATOM 781 O VAL A 104 20.671 6.711 −18.747 1.00 11.44 O ATOM 782 CB VAL A 104 19.385 9.603 −17.171 1.00 11.44 C ATOM 783 CG1 VAL A 104 18.070 8.866 −17.114 1.00 11.44 C ATOM 784 CG2 VAL A 104 19.557 10.430 −15.923 1.00 11.44 C ATOM 785 N ASP A 105 20.438 8.713 −19.737 1.00 34.00 N ATOM 786 CA ASP A 105 20.464 8.197 −21.104 1.00 34.00 C ATOM 787 C ASP A 105 21.365 6.995 −21.219 1.00 34.00 C ATOM 788 O ASP A 105 21.022 5.999 −21.850 1.00 34.00 O ATOM 789 CB ASP A 105 21.007 9.260 −22.045 1.00 34.00 C ATOM 790 CG ASP A 105 20.138 10.467 −22.101 1.00 34.00 C ATOM 791 OD1 ASP A 105 18.915 10.295 −22.281 1.00 34.00 O ATOM 792 OD2 ASP A 105 20.676 11.583 −21.966 1.00 34.00 O ATOM 793 N SER A 106 22.538 7.114 −20.615 1.00 14.20 N ATOM 794 CA SER A 106 23.542 6.066 −20.665 1.00 14.20 C ATOM 795 C SER A 106 23.034 4.769 −20.040 1.00 14.20 C ATOM 796 O SER A 106 22.929 3.743 −20.705 1.00 14.20 O ATOM 797 CB SER A 106 24.811 6.551 −19.968 1.00 14.20 C ATOM 798 OG SER A 106 25.141 7.859 −20.409 1.00 14.20 O ATOM 799 N MET A 107 22.725 4.829 −18.755 1.00 15.01 N ATOM 800 CA MET A 107 22.135 3.703 −18.050 1.00 15.01 C ATOM 801 C MET A 107 20.886 3.273 −18.793 1.00 15.01 C ATOM 802 O MET A 107 20.539 2.087 −18.846 1.00 15.01 O ATOM 803 CB MET A 107 21.747 4.144 −16.637 1.00 15.01 C ATOM 804 CG MET A 107 21.215 3.046 −15.754 1.00 15.01 C ATOM 805 SD MET A 107 22.537 1.930 −15.333 1.00 15.01 S ATOM 806 CE MET A 107 23.900 3.072 −15.193 1.00 15.01 C ATOM 807 N GLN A 108 20.217 4.265 −19.363 1.00 37.64 N ATOM 808 CA GLN A 108 18.928 4.068 −19.992 1.00 37.64 C ATOM 809 C GLN A 108 19.064 3.140 −21.197 1.00 37.64 C ATOM 810 O GLN A 108 18.259 2.229 −21.379 1.00 37.64 O ATOM 811 CB GLN A 108 18.313 5.420 −20.376 1.00 37.64 C ATOM 812 CG GLN A 108 16.861 5.343 −20.818 1.00 37.64 C ATOM 813 CD GLN A 108 16.012 4.507 −19.873 1.00 37.64 C ATOM 814 OE1 GLN A 108 16.447 4.157 −18.772 1.00 37.64 O ATOM 815 NE2 GLN A 108 14.794 4.176 −20.301 1.00 37.64 N ATOM 816 N LYS A 109 20.096 3.366 −22.005 1.00 58.25 N ATOM 817 CA LYS A 109 20.456 2.432 −23.064 1.00 58.25 C ATOM 818 C LYS A 109 20.519 1.022 −22.510 1.00 58.25 C ATOM 819 O LYS A 109 19.783 0.136 −22.946 1.00 58.25 O ATOM 820 CB LYS A 109 21.833 2.762 −23.627 1.00 58.25 C ATOM 821 CG LYS A 109 22.610 1.514 −24.080 1.00 58.25 C ATOM 822 CD LYS A 109 22.107 0.977 −25.420 1.00 58.25 C ATOM 823 CE LYS A 109 22.947 1.493 −26.604 1.00 58.25 C ATOM 824 NZ LYS A 109 23.371 2.931 −26.501 1.00 58.25 N ATOM 825 N ASP A 110 21.429 0.827 −21.559 1.00 26.08 N ATOM 826 CA ASP A 110 21.685 −0.478 −20.968 1.00 26.08 C ATOM 827 C ASP A 110 20.403 −1.115 −20.497 1.00 26.08 C ATOM 828 O ASP A 110 20.351 −2.324 −20.286 1.00 26.08 O ATOM 829 CB ASP A 110 22.644 −0.357 −19.791 1.00 26.08 C ATOM 830 CG ASP A 110 24.085 −0.220 −20.228 1.00 26.08 C ATOM 831 OD1 ASP A 110 24.339 0.349 −21.316 1.00 26.08 O ATOM 832 OD2 ASP A 110 24.966 −0.680 −19.474 1.00 26.08 O ATOM 833 N TYR A 111 19.371 −0.303 −20.306 1.00 34.27 N ATOM 834 CA TYR A 111 18.084 −0.846 −19.902 1.00 34.27 C ATOM 835 C TYR A 111 16.945 −0.200 −20.668 1.00 34.27 C ATOM 836 O TYR A 111 16.175 0.581 −20.118 1.00 34.27 O ATOM 837 CB TYR A 111 17.904 −0.733 −18.392 1.00 34.27 C ATOM 838 CG TYR A 111 19.005 −1.433 −17.642 1.00 34.27 C ATOM 839 CD1 TYR A 111 20.161 −0.757 −17.285 1.00 34.27 C ATOM 840 CD2 TYR A 111 18.905 −2.777 −17.316 1.00 34.27 C ATOM 841 CE1 TYR A 111 21.185 −1.399 −16.600 1.00 34.27 C ATOM 842 CE2 TYR A 111 19.921 −3.431 −16.634 1.00 34.27 C ATOM 843 CZ TYR A 111 21.060 −2.741 −16.276 1.00 34.27 C ATOM 844 OH TYR A 111 22.076 −3.383 −15.595 1.00 34.27 O ATOM 845 N PRO A 112 16.828 −0.552 −21.950 1.00 27.06 N ATOM 846 CA PRO A 112 15.828 0.043 −22.830 1.00 27.06 C ATOM 847 C PRO A 112 14.461 −0.436 −22.409 1.00 27.06 C ATOM 848 O PRO A 112 14.361 −1.475 −21.758 1.00 27.06 O ATOM 849 CB PRO A 112 16.170 −0.548 −24.202 1.00 27.06 C ATOM 850 CG PRO A 112 17.444 −1.320 −24.019 1.00 27.06 C ATOM 851 CD PRO A 112 17.502 −1.689 −22.584 1.00 27.06 C ATOM 852 N GLY A 113 13.425 0.304 −22.783 1.00 56.90 N ATOM 853 CA GLY A 113 12.072 −0.076 −22.439 1.00 56.90 C ATOM 854 C GLY A 113 11.948 −0.289 −20.948 1.00 56.90 C ATOM 855 O GLY A 113 11.009 −0.926 −20.479 1.00 56.90 O ATOM 856 N LEU A 114 12.911 0.236 −20.200 1.00 47.92 N ATOM 857 CA LEU A 114 12.851 0.198 −18.748 1.00 47.92 C ATOM 858 C LEU A 114 12.566 1.608 −18.233 1.00 47.92 C ATOM 859 O LEU A 114 13.165 2.580 −18.699 1.00 47.92 O ATOM 860 CB LEU A 114 14.158 −0.337 −18.175 1.00 47.92 C ATOM 861 CG LEU A 114 14.024 −1.068 −16.851 1.00 47.92 C ATOM 862 CD1 LEU A 114 12.930 −2.109 −16.952 1.00 47.92 C ATOM 863 CD2 LEU A 114 15.343 −1.707 −16.478 1.00 47.92 C ATOM 864 N PRO A 115 11.630 1.726 −17.282 1.00 10.78 N ATOM 865 CA PRO A 115 11.120 2.998 −16.759 1.00 10.78 C ATOM 866 C PRO A 115 12.139 3.703 −15.890 1.00 10.78 C ATOM 867 O PRO A 115 12.971 3.033 −15.291 1.00 10.78 O ATOM 868 CB PRO A 115 9.933 2.569 −15.895 1.00 10.78 C ATOM 869 CG PRO A 115 9.621 1.177 −16.313 1.00 10.78 C ATOM 870 CD PRO A 115 10.926 0.579 −16.698 1.00 10.78 C ATOM 871 N VAL A 116 12.052 5.025 −15.793 1.00 28.93 N ATOM 872 CA VAL A 116 13.069 5.791 −15.086 1.00 28.93 C ATOM 873 C VAL A 116 12.506 6.857 −14.145 1.00 28.93 C ATOM 874 O VAL A 116 11.686 7.685 −14.540 1.00 28.93 O ATOM 875 CB VAL A 116 14.018 6.467 −16.078 1.00 28.93 C ATOM 876 CG1 VAL A 116 13.214 7.247 −17.108 1.00 28.93 C ATOM 877 CG2 VAL A 116 15.004 7.365 −15.344 1.00 28.93 C ATOM 878 N PHE A 117 12.978 6.834 −12.903 1.00 16.78 N ATOM 879 CA PHE A 117 12.566 7.787 −11.876 1.00 16.78 C ATOM 880 C PHE A 117 13.661 8.813 −11.534 1.00 16.78 C ATOM 881 O PHE A 117 14.730 8.829 −12.143 1.00 16.78 O ATOM 882 CB PHE A 117 12.172 7.031 −10.606 1.00 16.78 C ATOM 883 CG PHE A 117 10.951 6.167 −10.763 1.00 16.78 C ATOM 884 CD1 PHE A 117 11.042 4.900 −11.320 1.00 16.78 C ATOM 885 CD2 PHE A 117 9.705 6.619 −10.338 1.00 16.78 C ATOM 886 CE1 PHE A 117 9.914 4.110 −11.458 1.00 16.78 C ATOM 887 CE2 PHE A 117 8.578 5.835 −10.472 1.00 16.78 C ATOM 888 CZ PHE A 117 8.682 4.585 −11.031 1.00 16.78 C ATOM 889 N LEU A 118 13.377 9.662 −10.548 1.00 8.59 N ATOM 890 CA LEU A 118 14.338 10.631 −10.034 1.00 8.59 C ATOM 891 C LEU A 118 14.120 10.829 −8.538 1.00 8.59 C ATOM 892 O LEU A 118 12.988 10.802 −8.070 1.00 8.59 O ATOM 893 CB LEU A 118 14.172 11.970 −10.734 1.00 8.59 C ATOM 894 CG LEU A 118 14.796 12.044 −12.115 1.00 8.59 C ATOM 895 CD1 LEU A 118 14.647 13.444 −12.680 1.00 8.59 C ATOM 896 CD2 LEU A 118 16.247 11.658 −12.013 1.00 8.59 C ATOM 897 N LEU A 119 15.202 11.026 −7.788 1.00 10.47 N ATOM 898 CA LEU A 119 15.110 11.338 −6.363 1.00 10.47 C ATOM 899 C LEU A 119 16.183 12.354 −6.013 1.00 10.47 C ATOM 900 O LEU A 119 17.353 12.155 −6.303 1.00 10.47 O ATOM 901 CB LEU A 119 15.287 10.071 −5.523 1.00 10.47 C ATOM 902 CG LEU A 119 14.996 10.108 −4.014 1.00 10.47 C ATOM 903 CD1 LEU A 119 14.674 8.709 −3.511 1.00 10.47 C ATOM 904 CD2 LEU A 119 16.134 10.734 −3.196 1.00 10.47 C ATOM 905 N GLY A 120 15.790 13.455 −5.400 1.00 4.13 N ATOM 906 CA GLY A 120 16.759 14.453 −4.999 1.00 4.13 C ATOM 907 C GLY A 120 16.446 15.045 −3.642 1.00 4.13 C ATOM 908 O GLY A 120 15.322 14.958 −3.157 1.00 4.13 O ATOM 909 N HIS A 121 17.443 15.645 −3.018 1.00 6.73 N ATOM 910 CA HIS A 121 17.202 16.309 −1.761 1.00 6.73 C ATOM 911 C HIS A 121 17.681 17.744 −1.864 1.00 6.73 C ATOM 912 O HIS A 121 18.735 18.006 −2.432 1.00 6.73 O ATOM 913 CB HIS A 121 17.885 15.568 −0.615 1.00 6.73 C ATOM 914 CG HIS A 121 17.880 16.323 0.676 1.00 6.73 C ATOM 915 ND1 HIS A 121 16.832 17.128 1.063 1.00 6.73 N ATOM 916 CD2 HIS A 121 18.793 16.390 1.672 1.00 6.73 C ATOM 917 CE1 HIS A 121 17.101 17.664 2.240 1.00 6.73 C ATOM 918 NE2 HIS A 121 18.285 17.233 2.630 1.00 6.73 N ATOM 919 N SER A 122 16.883 18.667 −1.333 1.00 5.10 N ATOM 920 CA SER A 122 17.189 20.095 −1.368 1.00 5.10 C ATOM 921 C SER A 122 17.668 20.592 −2.730 1.00 5.10 C ATOM 922 O SER A 122 16.860 20.744 −3.648 1.00 5.10 O ATOM 923 CB SER A 122 18.178 20.464 −0.271 1.00 5.10 C ATOM 924 OG SER A 122 19.073 19.403 −0.048 1.00 5.10 O ATOM 925 N MET A 123 18.965 20.868 −2.857 1.00 30.42 N ATOM 926 CA MET A 123 19.516 21.308 −4.135 1.00 30.42 C ATOM 927 C MET A 123 19.589 20.131 −5.091 1.00 30.42 C ATOM 928 O MET A 123 19.609 20.301 −6.309 1.00 30.42 O ATOM 929 CB MET A 123 20.902 21.931 −3.972 1.00 30.42 C ATOM 930 CG MET A 123 21.456 22.532 −5.274 1.00 30.42 C ATOM 931 SD MET A 123 23.262 22.560 −5.420 1.00 30.42 S ATOM 932 CE MET A 123 23.654 20.815 −5.637 1.00 30.42 C ATOM 933 N GLY A 124 19.641 18.930 −4.532 1.00 12.27 N ATOM 934 CA GLY A 124 19.528 17.740 −5.342 1.00 12.27 C ATOM 935 C GLY A 124 18.177 17.790 −6.001 1.00 12.27 C ATOM 936 O GLY A 124 18.058 17.583 −7.198 1.00 12.27 O ATOM 937 N GLY A 125 17.157 18.074 −5.202 1.00 17.40 N ATOM 938 CA GLY A 125 15.813 18.240 −5.713 1.00 17.40 C ATOM 939 C GLY A 125 15.777 19.225 −6.863 1.00 17.40 C ATOM 940 O GLY A 125 15.503 18.848 −8.006 1.00 17.40 O ATOM 941 N ALA A 126 16.046 20.490 −6.560 1.00 16.05 N ATOM 942 CA ALA A 126 16.095 21.535 −7.579 1.00 16.05 C ATOM 943 C ALA A 126 16.579 20.993 −8.923 1.00 16.05 C ATOM 944 O ALA A 126 15.908 21.135 −9.950 1.00 16.05 O ATOM 945 CB ALA A 126 16.980 22.668 −7.118 1.00 16.05 C ATOM 946 N ILE A 127 17.748 20.367 −8.898 1.00 12.02 N ATOM 947 CA ILE A 127 18.299 19.710 −10.069 1.00 12.02 C ATOM 948 C ILE A 127 17.299 18.745 −10.719 1.00 12.02 C ATOM 949 O ILE A 127 16.838 18.975 −11.843 1.00 12.02 O ATOM 950 CB ILE A 127 19.576 18.965 −9.696 1.00 12.02 C ATOM 951 CG1 ILE A 127 20.660 19.965 −9.323 1.00 12.02 C ATOM 952 CG2 ILE A 127 20.037 18.089 −10.839 1.00 12.02 C ATOM 953 CD1 ILE A 127 21.857 19.331 −8.691 1.00 12.02 C ATOM 954 N ALA A 128 16.972 17.666 −10.013 1.00 7.84 N ATOM 955 CA ALA A 128 16.001 16.689 −10.491 1.00 7.84 C ATOM 956 C ALA A 128 14.797 17.383 −11.119 1.00 7.84 C ATOM 957 O ALA A 128 14.408 17.079 −12.239 1.00 7.84 O ATOM 958 CB ALA A 128 15.558 15.803 −9.347 1.00 7.84 C ATOM 959 N ILE A 129 14.210 18.319 −10.378 1.00 23.62 N ATOM 960 CA ILE A 129 13.112 19.136 −10.885 1.00 23.62 C ATOM 961 C ILE A 129 13.429 19.692 −12.259 1.00 23.62 C ATOM 962 O ILE A 129 12.758 19.369 −13.237 1.00 23.62 O ATOM 963 CB ILE A 129 12.809 20.320 −9.960 1.00 23.62 C ATOM 964 CG1 ILE A 129 11.898 19.880 −8.827 1.00 23.62 C ATOM 965 CG2 ILE A 129 12.120 21.426 −10.729 1.00 23.62 C ATOM 966 CD1 ILE A 129 11.504 21.010 −7.913 1.00 23.62 C ATOM 967 N LEU A 130 14.454 20.536 −12.323 1.00 6.40 N ATOM 968 CA LEU A 130 14.853 21.154 −13.575 1.00 6.40 C ATOM 969 C LEU A 130 15.181 20.128 −14.660 1.00 6.40 C ATOM 970 O LEU A 130 15.123 20.444 −15.853 1.00 6.40 O ATOM 971 CB LEU A 130 16.034 22.097 −13.357 1.00 6.40 C ATOM 972 CG LEU A 130 15.678 23.372 −12.598 1.00 6.40 C ATOM 973 CD1 LEU A 130 16.717 24.458 −12.807 1.00 6.40 C ATOM 974 CD2 LEU A 130 14.317 23.857 −13.035 1.00 6.40 C ATOM 975 N THR A 131 15.509 18.903 −14.253 1.00 6.12 N ATOM 976 CA THR A 131 15.868 17.878 −15.217 1.00 6.12 C ATOM 977 C THR A 131 14.647 17.331 −15.914 1.00 6.12 C ATOM 978 O THR A 131 14.747 16.782 −17.000 1.00 6.12 O ATOM 979 CB THR A 131 16.603 16.716 −14.572 1.00 6.12 C ATOM 980 OG1 THR A 131 17.829 17.186 −14.006 1.00 6.12 O ATOM 981 CG2 THR A 131 16.924 15.666 −15.611 1.00 6.12 C ATOM 982 N ALA A 132 13.492 17.468 −15.281 1.00 13.33 N ATOM 983 CA ALA A 132 12.251 17.014 −15.890 1.00 13.33 C ATOM 984 C ALA A 132 11.751 18.075 −16.859 1.00 13.33 C ATOM 985 O ALA A 132 11.036 17.781 −17.813 1.00 13.33 O ATOM 986 CB ALA A 132 11.216 16.729 −14.824 1.00 13.33 C ATOM 987 N ALA A 133 12.148 19.316 −16.600 1.00 26.88 N ATOM 988 CA ALA A 133 11.822 20.440 −17.468 1.00 26.88 C ATOM 989 C ALA A 133 12.317 20.169 −18.878 1.00 26.88 C ATOM 990 O ALA A 133 11.761 20.660 −19.856 1.00 26.88 O ATOM 991 CB ALA A 133 12.440 21.717 −16.924 1.00 26.88 C ATOM 992 N GLU A 134 13.364 19.364 −18.969 1.00 24.35 N ATOM 993 CA GLU A 134 14.021 19.121 −20.237 1.00 24.35 C ATOM 994 C GLU A 134 13.505 17.879 −20.950 1.00 24.35 C ATOM 995 O GLU A 134 13.452 17.849 −22.176 1.00 24.35 O ATOM 996 CB GLU A 134 15.527 19.032 −20.021 1.00 24.35 C ATOM 997 CG GLU A 134 16.314 18.753 −21.274 1.00 24.35 C ATOM 998 CD GLU A 134 17.727 19.236 −21.145 1.00 24.35 C ATOM 999 OE1 GLU A 134 17.997 19.991 −20.183 1.00 24.35 O ATOM 1000 OE2 GLU A 134 18.557 18.862 −22.001 1.00 24.35 O ATOM 1001 N ARG A 135 13.121 16.860 −20.188 1.00 22.63 N ATOM 1002 CA ARG A 135 12.572 15.637 −20.775 1.00 22.63 C ATOM 1003 C ARG A 135 11.112 15.428 −20.385 1.00 22.63 C ATOM 1004 O ARG A 135 10.772 14.424 −19.765 1.00 22.63 O ATOM 1005 CB ARG A 135 13.390 14.397 −20.380 1.00 22.63 C ATOM 1006 CG ARG A 135 14.885 14.493 −20.649 1.00 22.63 C ATOM 1007 CD ARG A 135 15.250 14.069 −22.054 1.00 22.63 C ATOM 1008 NE ARG A 135 16.481 14.715 −22.499 1.00 22.63 N ATOM 1009 CZ ARG A 135 17.678 14.139 −22.483 1.00 22.63 C ATOM 1010 NH1 ARG A 135 17.793 12.894 −22.047 1.00 22.63 N ATOM 1011 NH2 ARG A 135 18.751 14.807 −22.904 1.00 22.63 N ATOM 1012 N PRO A 136 10.242 16.374 −20.759 1.00 11.69 N ATOM 1013 CA PRO A 136 8.814 16.212 −20.484 1.00 11.69 C ATOM 1014 C PRO A 136 8.288 14.870 −20.974 1.00 11.69 C ATOM 1015 O PRO A 136 8.288 14.611 −22.171 1.00 11.69 O ATOM 1016 CB PRO A 136 8.175 17.338 −21.297 1.00 11.69 C ATOM 1017 CG PRO A 136 9.231 18.364 −21.413 1.00 11.69 C ATOM 1018 CD PRO A 136 10.530 17.628 −21.475 1.00 11.69 C ATOM 1019 N GLY A 137 7.839 14.027 −20.057 1.00 4.28 N ATOM 1020 CA GLY A 137 7.202 12.792 −20.449 1.00 4.28 C ATOM 1021 C GLY A 137 8.161 11.625 −20.505 1.00 4.28 C ATOM 1022 O GLY A 137 7.751 10.495 −20.750 1.00 4.28 O ATOM 1023 N HIS A 138 9.437 11.885 −20.266 1.00 23.62 N ATOM 1024 CA HIS A 138 10.399 10.804 −20.211 1.00 23.62 C ATOM 1025 C HIS A 138 10.295 10.026 −18.896 1.00 23.62 C ATOM 1026 O HIS A 138 10.132 8.799 −18.894 1.00 23.62 O ATOM 1027 CB HIS A 138 11.815 11.336 −20.396 1.00 23.62 C ATOM 1028 CG HIS A 138 12.821 10.267 −20.693 1.00 23.62 C ATOM 1029 ND1 HIS A 138 13.796 10.405 −21.657 1.00 23.62 N ATOM 1030 CD2 HIS A 138 12.984 9.026 −20.170 1.00 23.62 C ATOM 1031 CE1 HIS A 138 14.532 9.307 −21.697 1.00 23.62 C ATOM 1032 NE2 HIS A 138 14.060 8.454 −20.805 1.00 23.62 N ATOM 1033 N PHE A 139 10.380 10.746 −17.779 1.00 24.36 N ATOM 1034 CA PHE A 139 10.471 10.118 −16.460 1.00 24.36 C ATOM 1035 C PHE A 139 9.147 9.604 −15.916 1.00 24.36 C ATOM 1036 O PHE A 139 8.112 10.267 −16.027 1.00 24.36 O ATOM 1037 CB PHE A 139 11.075 11.081 −15.449 1.00 24.36 C ATOM 1038 CG PHE A 139 12.428 11.586 −15.831 1.00 24.36 C ATOM 1039 CD1 PHE A 139 13.508 10.717 −15.902 1.00 24.36 C ATOM 1040 CD2 PHE A 139 12.626 12.938 −16.105 1.00 24.36 C ATOM 1041 CE1 PHE A 139 14.753 11.179 −16.248 1.00 24.36 C ATOM 1042 CE2 PHE A 139 13.875 13.404 −16.449 1.00 24.36 C ATOM 1043 CZ PHE A 139 14.937 12.521 −16.519 1.00 24.36 C ATOM 1044 N ALA A 140 9.201 8.425 −15.304 1.00 22.82 N ATOM 1045 CA ALA A 140 8.023 7.798 −14.727 1.00 22.82 C ATOM 1046 C ALA A 140 7.527 8.556 −13.496 1.00 22.82 C ATOM 1047 O ALA A 140 6.330 8.579 −13.208 1.00 22.82 O ATOM 1048 CB ALA A 140 8.313 6.356 −14.383 1.00 22.82 C ATOM 1049 N GLY A 141 8.450 9.175 −12.770 1.00 14.94 N ATOM 1050 CA GLY A 141 8.081 9.942 −11.594 1.00 14.94 C ATOM 1051 C GLY A 141 9.286 10.352 −10.783 1.00 14.94 C ATOM 1052 O GLY A 141 10.331 9.721 −10.872 1.00 14.94 O ATOM 1053 N MET A 142 9.151 11.410 −9.993 1.00 10.49 N ATOM 1054 CA MET A 142 10.268 11.853 −9.166 1.00 10.49 C ATOM 1055 C MET A 142 9.899 12.078 −7.698 1.00 10.49 C ATOM 1056 O MET A 142 8.951 12.782 −7.386 1.00 10.49 O ATOM 1057 CB MET A 142 10.905 13.106 −9.754 1.00 10.49 C ATOM 1058 CG MET A 142 9.976 14.282 −9.801 1.00 10.49 C ATOM 1059 SD MET A 142 10.833 15.813 −10.153 1.00 10.49 S ATOM 1060 CE MET A 142 9.457 16.954 −10.104 1.00 10.49 C ATOM 1061 N VAL A 143 10.660 11.461 −6.802 1.00 10.87 N ATOM 1062 CA VAL A 143 10.477 11.618 −5.364 1.00 10.87 C ATOM 1063 C VAL A 143 11.391 12.731 −4.921 1.00 10.87 C ATOM 1064 O VAL A 143 12.585 12.685 −5.209 1.00 10.87 O ATOM 1065 CB VAL A 143 10.901 10.359 −4.591 1.00 10.87 C ATOM 1066 CG1 VAL A 143 11.139 10.691 −3.137 1.00 10.87 C ATOM 1067 CG2 VAL A 143 9.870 9.281 −4.732 1.00 10.87 C ATOM 1068 N LEU A 144 10.844 13.712 −4.208 1.00 7.18 N ATOM 1069 CA LEU A 144 11.618 14.871 −3.806 1.00 7.18 C ATOM 1070 C LEU A 144 11.588 15.079 −2.304 1.00 7.18 C ATOM 1071 O LEU A 144 10.518 15.263 −1.728 1.00 7.18 O ATOM 1072 CB LEU A 144 11.056 16.101 −4.495 1.00 7.18 C ATOM 1073 CG LEU A 144 11.354 16.169 −5.991 1.00 7.18 C ATOM 1074 CD1 LEU A 144 10.201 16.815 −6.746 1.00 7.18 C ATOM 1075 CD2 LEU A 144 12.659 16.902 −6.228 1.00 7.18 C ATOM 1076 N ILE A 145 12.756 15.061 −1.666 1.00 5.05 N ATOM 1077 CA ILE A 145 12.827 15.302 −0.226 1.00 5.05 C ATOM 1078 C ILE A 145 13.221 16.746 0.052 1.00 5.05 C ATOM 1079 O ILE A 145 14.343 17.165 −0.238 1.00 5.05 O ATOM 1080 CB ILE A 145 13.796 14.342 0.484 1.00 5.05 C ATOM 1081 CG1 ILE A 145 13.422 12.885 0.183 1.00 5.05 C ATOM 1082 CG2 ILE A 145 13.777 14.583 1.978 1.00 5.05 C ATOM 1083 CD1 ILE A 145 14.590 11.918 0.215 1.00 5.05 C ATOM 1084 N SER A 146 12.279 17.499 0.613 1.00 14.94 N ATOM 1085 CA SER A 146 12.434 18.929 0.815 1.00 14.94 C ATOM 1086 C SER A 146 13.441 19.521 −0.164 1.00 14.94 C ATOM 1087 O SER A 146 14.479 20.026 0.244 1.00 14.94 O ATOM 1088 CB SER A 146 12.817 19.248 2.269 1.00 14.94 C ATOM 1089 OG SER A 146 14.011 18.601 2.667 1.00 14.94 O ATOM 1090 N PRO A 147 13.129 19.466 −1.467 1.00 6.17 N ATOM 1091 CA PRO A 147 13.961 20.082 −2.501 1.00 6.17 C ATOM 1092 C PRO A 147 14.070 21.583 −2.317 1.00 6.17 C ATOM 1093 O PRO A 147 13.307 22.192 −1.564 1.00 6.17 O ATOM 1094 CB PRO A 147 13.171 19.806 −3.782 1.00 6.17 C ATOM 1095 CG PRO A 147 11.762 19.598 −3.317 1.00 6.17 C ATOM 1096 CD PRO A 147 11.959 18.802 −2.065 1.00 6.17 C ATOM 1097 N LEU A 148 15.020 22.174 −3.026 1.00 15.73 N ATOM 1098 CA LEU A 148 15.244 23.603 −2.964 1.00 15.73 C ATOM 1099 C LEU A 148 14.380 24.307 −3.990 1.00 15.73 C ATOM 1100 O LEU A 148 14.781 24.528 −5.128 1.00 15.73 O ATOM 1101 CB LEU A 148 16.713 23.933 −3.203 1.00 15.73 C ATOM 1102 CG LEU A 148 16.964 25.411 −3.502 1.00 15.73 C ATOM 1103 CD1 LEU A 148 16.487 26.287 −2.343 1.00 15.73 C ATOM 1104 CD2 LEU A 148 18.435 25.660 −3.828 1.00 15.73 C ATOM 1105 N VAL A 149 13.176 24.649 −3.581 1.00 5.98 N ATOM 1106 CA VAL A 149 12.314 25.448 −4.416 1.00 5.98 C ATOM 1107 C VAL A 149 12.524 26.913 −4.043 1.00 5.98 C ATOM 1108 O VAL A 149 13.079 27.694 −4.819 1.00 5.98 O ATOM 1109 CB VAL A 149 10.866 25.038 −4.203 1.00 5.98 C ATOM 1110 CG1 VAL A 149 9.936 25.950 −4.967 1.00 5.98 C ATOM 1111 CG2 VAL A 149 10.687 23.614 −4.651 1.00 5.98 C ATOM 1112 N LEU A 150 12.070 27.263 −2.844 1.00 22.90 N ATOM 1113 CA LEU A 150 12.367 28.540 −2.219 1.00 22.90 C ATOM 1114 C LEU A 150 13.149 28.225 −0.964 1.00 22.90 C ATOM 1115 O LEU A 150 12.875 27.223 −0.304 1.00 22.90 O ATOM 1116 CB LEU A 150 11.075 29.238 −1.819 1.00 22.90 C ATOM 1117 CG LEU A 150 10.277 29.979 −2.885 1.00 22.90 C ATOM 1118 CD1 LEU A 150 10.732 29.631 −4.288 1.00 22.90 C ATOM 1119 CD2 LEU A 150 8.791 29.702 −2.692 1.00 22.90 C ATOM 1120 N ALA A 151 14.112 29.073 −0.624 1.00 26.17 N ATOM 1121 CA ALA A 151 14.928 28.847 0.565 1.00 26.17 C ATOM 1122 C ALA A 151 14.606 29.841 1.666 1.00 26.17 C ATOM 1123 O ALA A 151 14.258 30.982 1.375 1.00 26.17 O ATOM 1124 CB ALA A 151 16.390 28.924 0.215 1.00 26.17 C ATOM 1125 N ASN A 152 14.713 29.398 2.918 1.00 26.58 N ATOM 1126 CA ASN A 152 14.620 30.276 4.077 1.00 26.58 C ATOM 1127 C ASN A 152 15.093 31.635 3.634 1.00 26.58 C ATOM 1128 O ASN A 152 16.010 31.726 2.832 1.00 26.58 O ATOM 1129 CB ASN A 152 15.540 29.766 5.182 1.00 26.58 C ATOM 1130 CG ASN A 152 15.083 30.171 6.580 1.00 26.58 C ATOM 1131 OD1 ASN A 152 15.899 30.564 7.419 1.00 26.58 O ATOM 1132 ND2 ASN A 152 13.784 30.057 6.842 1.00 26.58 N ATOM 1133 N PRO A 153 14.466 32.699 4.138 1.00 61.45 N ATOM 1134 CA PRO A 153 14.704 34.058 3.644 1.00 61.45 C ATOM 1135 C PRO A 153 15.741 34.859 4.449 1.00 61.45 C ATOM 1136 O PRO A 153 15.383 35.941 4.881 1.00 61.45 O ATOM 1137 CB PRO A 153 13.332 34.735 3.833 1.00 61.45 C ATOM 1138 CG PRO A 153 12.422 33.696 4.482 1.00 61.45 C ATOM 1139 CD PRO A 153 13.316 32.645 5.046 1.00 61.45 C ATOM 1140 N GLU A 154 16.973 34.404 4.679 1.00 63.32 N ATOM 1141 CA GLU A 154 17.587 33.285 4.001 1.00 63.32 C ATOM 1142 C GLU A 154 18.225 32.257 4.951 1.00 63.32 C ATOM 1143 CB GLU A 154 18.623 33.816 3.014 1.00 63.32 C ATOM 1144 CG GLU A 154 18.325 35.229 2.510 1.00 63.32 C ATOM 1145 CD GLU A 154 17.186 35.301 1.496 1.00 63.32 C ATOM 1146 OE1 GLU A 154 17.075 36.355 0.831 1.00 63.32 O ATOM 1147 OE2 GLU A 154 16.411 34.326 1.354 1.00 63.32 O ATOM 1148 O GLU A 154 18.174 32.381 6.182 1.00 63.32 O ATOM 1149 N SER A 155 18.840 31.250 4.342 1.00 22.65 N ATOM 1150 CA SER A 155 19.345 30.082 5.027 1.00 22.65 C ATOM 1151 C SER A 155 20.847 30.206 5.038 1.00 22.65 C ATOM 1152 CB SER A 155 18.933 28.894 4.202 1.00 22.65 C ATOM 1153 OG SER A 155 17.869 29.300 3.362 1.00 22.65 O ATOM 1154 O SER A 155 21.541 29.645 5.880 1.00 22.65 O ATOM 1155 N ALA A 156 21.346 30.953 4.071 1.00 18.66 N ATOM 1156 CA ALA A 156 22.713 31.412 4.101 1.00 18.66 C ATOM 1157 C ALA A 156 22.686 32.925 3.932 1.00 18.66 C ATOM 1158 CB ALA A 156 23.523 30.757 3.002 1.00 18.66 C ATOM 1159 O ALA A 156 21.906 33.467 3.134 1.00 18.66 O ATOM 1160 N THR A 157 23.520 33.601 4.712 1.00 33.47 N ATOM 1161 CA THR A 157 23.674 35.042 4.613 1.00 33.47 C ATOM 1162 C THR A 157 24.177 35.371 3.208 1.00 33.47 C ATOM 1163 CB THR A 157 24.651 35.541 5.699 1.00 33.47 C ATOM 1164 OG1 THR A 157 24.125 35.212 6.993 1.00 33.47 O ATOM 1165 CG2 THR A 157 24.881 37.047 5.597 1.00 33.47 C ATOM 1166 O THR A 157 24.095 36.514 2.745 1.00 33.47 O ATOM 1167 N THR A 158 24.680 34.336 2.536 1.00 11.14 N ATOM 1168 CA THR A 158 25.142 34.418 1.155 1.00 11.14 C ATOM 1169 C THR A 158 24.064 34.960 0.213 1.00 11.14 C ATOM 1170 CB THR A 158 25.606 33.033 0.654 1.00 11.14 C ATOM 1171 OG1 THR A 158 26.194 32.299 1.739 1.00 11.14 O ATOM 1172 CG2 THR A 158 26.610 33.166 −0.495 1.00 11.14 C ATOM 1173 O THR A 158 24.365 35.484 −0.857 1.00 11.14 O ATOM 1174 N PHE A 159 22.805 34.832 0.609 1.00 22.19 N ATOM 1175 CA PHE A 159 21.731 35.441 −0.161 1.00 22.19 C ATOM 1176 C PHE A 159 21.632 36.921 0.177 1.00 22.19 C ATOM 1177 CB PHE A 159 20.401 34.738 0.092 1.00 22.19 C ATOM 1178 CG PHE A 159 20.396 33.286 −0.309 1.00 22.19 C ATOM 1179 CD1 PHE A 159 20.952 32.884 −1.511 1.00 22.19 C ATOM 1180 CD2 PHE A 159 19.817 32.325 0.510 1.00 22.19 C ATOM 1181 CE1 PHE A 159 20.942 31.551 −1.879 1.00 22.19 C ATOM 1182 CE2 PHE A 159 19.799 30.996 0.144 1.00 22.19 C ATOM 1183 CZ PHE A 159 20.365 30.607 −1.049 1.00 22.19 C ATOM 1184 O PHE A 159 21.802 37.774 −0.696 1.00 22.19 O ATOM 1185 N LYS A 160 21.373 37.216 1.449 1.00 7.97 N ATOM 1186 CA LYS A 160 21.364 38.595 1.925 1.00 7.97 C ATOM 1187 C LYS A 160 22.419 39.415 1.207 1.00 7.97 C ATOM 1188 CB LYS A 160 21.597 38.664 3.438 1.00 7.97 C ATOM 1189 CG LYS A 160 20.335 38.584 4.252 1.00 7.97 C ATOM 1190 CD LYS A 160 20.625 38.123 5.655 1.00 7.97 C ATOM 1191 CE LYS A 160 19.430 37.423 6.259 1.00 7.97 C ATOM 1192 NZ LYS A 160 19.743 36.981 7.631 1.00 7.97 N ATOM 1193 O LYS A 160 22.157 40.551 0.808 1.00 7.97 O ATOM 1194 N VAL A 161 23.608 38.841 1.034 1.00 28.88 N ATOM 1195 CA VAL A 161 24.702 39.578 0.412 1.00 28.88 C ATOM 1196 C VAL A 161 24.587 39.690 −1.100 1.00 28.88 C ATOM 1197 CB VAL A 161 26.081 39.007 0.769 1.00 28.88 C ATOM 1198 CG1 VAL A 161 27.162 39.648 −0.109 1.00 28.88 C ATOM 1199 CG2 VAL A 161 26.086 37.513 0.614 1.00 28.88 C ATOM 1200 O VAL A 161 24.782 40.768 −1.656 1.00 28.88 O ATOM 1201 N LEU A 162 24.289 38.581 −1.767 1.00 33.67 N ATOM 1202 CA LEU A 162 24.092 38.624 −3.207 1.00 33.67 C ATOM 1203 C LEU A 162 23.006 39.643 −3.484 1.00 33.67 C ATOM 1204 CB LEU A 162 23.673 37.258 −3.755 1.00 33.67 C ATOM 1205 CG LEU A 162 24.656 36.085 −3.685 1.00 33.67 C ATOM 1206 CD1 LEU A 162 23.901 34.776 −3.680 1.00 33.67 C ATOM 1207 CD2 LEU A 162 25.654 36.112 −4.828 1.00 33.67 C ATOM 1208 O LEU A 162 23.030 40.322 −4.509 1.00 33.67 O ATOM 1209 N ALA A 163 22.054 39.749 −2.559 1.00 15.92 N ATOM 1210 CA ALA A 163 20.945 40.694 −2.702 1.00 15.92 C ATOM 1211 C ALA A 163 21.327 42.076 −2.199 1.00 15.92 C ATOM 1212 CB ALA A 163 19.700 40.186 −1.985 1.00 15.92 C ATOM 1213 O ALA A 163 20.681 43.062 −2.529 1.00 15.92 O ATOM 1214 N ALA A 164 22.371 42.135 −1.380 1.00 40.99 N ATOM 1215 CA ALA A 164 22.974 43.400 −1.014 1.00 40.99 C ATOM 1216 C ALA A 164 23.560 43.967 −2.296 1.00 40.99 C ATOM 1217 CB ALA A 164 24.059 43.172 −0.001 1.00 40.99 C ATOM 1218 O ALA A 164 23.766 43.229 −3.255 1.00 40.99 O ATOM 1219 N LYS A 165 23.819 45.267 −2.340 1.00 10.25 N ATOM 1220 CA LYS A 165 24.536 45.829 −3.485 1.00 10.25 C ATOM 1221 C LYS A 165 25.909 46.310 −3.053 1.00 10.25 C ATOM 1222 CB LYS A 165 23.735 46.957 −4.136 1.00 10.25 C ATOM 1223 CG LYS A 165 22.883 46.503 −5.311 1.00 10.25 C ATOM 1224 CD LYS A 165 21.491 47.170 −5.350 1.00 10.25 C ATOM 1225 CE LYS A 165 21.545 48.695 −5.517 1.00 10.25 C ATOM 1226 NZ LYS A 165 20.202 49.332 −5.351 1.00 10.25 N ATOM 1227 O LYS A 165 26.134 47.506 −2.890 1.00 10.25 O ATOM 1228 N ALA A 166 26.825 45.365 −2.857 1.00 49.12 N ATOM 1229 CA ALA A 166 28.128 45.672 −2.276 1.00 49.12 C ATOM 1230 C ALA A 166 29.273 44.958 −2.987 1.00 49.12 C ATOM 1231 O ALA A 166 30.441 45.360 −2.881 1.00 49.12 O ATOM 1232 N LEU A 167 28.935 43.896 −3.708 1.00 17.91 N ATOM 1233 CA LEU A 167 29.933 43.143 −4.448 1.00 17.91 C ATOM 1234 C LEU A 167 30.465 44.014 −5.570 1.00 17.91 C ATOM 1235 CB LEU A 167 29.322 41.883 −5.064 1.00 17.91 C ATOM 1236 CG LEU A 167 28.719 40.779 −4.199 1.00 17.91 C ATOM 1237 CD1 LEU A 167 29.767 40.106 −3.340 1.00 17.91 C ATOM 1238 CD2 LEU A 167 28.028 39.766 −5.091 1.00 17.91 C ATOM 1239 O LEU A 167 29.757 44.905 −6.058 1.00 17.91 O ATOM 1240 N ASN A 168 31.712 43.772 −5.969 1.00 36.43 N ATOM 1241 CA ASN A 168 32.166 44.226 −7.275 1.00 36.43 C ATOM 1242 C ASN A 168 32.645 43.040 −8.098 1.00 36.43 C ATOM 1243 CB ASN A 168 33.234 45.328 −7.202 1.00 36.43 C ATOM 1244 CG ASN A 168 33.314 46.150 −8.498 1.00 36.43 C ATOM 1245 OD1 ASN A 168 32.428 46.080 −9.352 1.00 36.43 O ATOM 1246 ND2 ASN A 168 34.373 46.927 −8.641 1.00 36.43 N ATOM 1247 O ASN A 168 31.835 42.197 −8.515 1.00 36.43 O ATOM 1248 N SER A 169 33.956 42.960 −8.308 1.00 18.57 N ATOM 1249 CA SER A 169 34.483 42.031 −9.292 1.00 18.57 C ATOM 1250 C SER A 169 35.284 40.878 −8.711 1.00 18.57 C ATOM 1251 CB SER A 169 35.271 42.774 −10.366 1.00 18.57 C ATOM 1252 OG SER A 169 34.408 43.638 −11.092 1.00 18.57 O ATOM 1253 O SER A 169 35.868 40.973 −7.623 1.00 18.57 O ATOM 1254 N VAL A 170 35.271 39.788 −9.479 1.00 52.59 N ATOM 1255 CA VAL A 170 35.834 38.480 −9.133 1.00 52.59 C ATOM 1256 C VAL A 170 35.661 37.993 −7.683 1.00 52.59 C ATOM 1257 CB VAL A 170 37.277 38.317 −9.628 1.00 52.59 C ATOM 1258 CG1 VAL A 170 37.656 36.852 −9.612 1.00 52.59 C ATOM 1259 CG2 VAL A 170 37.417 38.883 −11.042 1.00 52.59 C ATOM 1260 O VAL A 170 35.922 36.821 −7.391 1.00 52.59 O ATOM 1261 N LEU A 171 35.234 38.879 −6.784 1.00 9.96 N ATOM 1262 CA LEU A 171 34.587 38.449 −5.549 1.00 9.96 C ATOM 1263 C LEU A 171 35.471 37.578 −4.649 1.00 9.96 C ATOM 1264 CB LEU A 171 33.307 37.666 −5.902 1.00 9.96 C ATOM 1265 CG LEU A 171 32.391 38.137 −7.045 1.00 9.96 C ATOM 1266 CD1 LEU A 171 31.801 36.968 −7.798 1.00 9.96 C ATOM 1267 CD2 LEU A 171 31.281 39.013 −6.528 1.00 9.96 C ATOM 1268 O LEU A 171 36.543 37.138 −5.067 1.00 9.96 O ATOM 1269 N PRO A 172 35.013 37.320 −3.407 1.00 7.00 N ATOM 1270 CA PRO A 172 35.673 36.405 −2.467 1.00 7.00 C ATOM 1271 C PRO A 172 35.624 34.953 −2.910 1.00 7.00 C ATOM 1272 CB PRO A 172 34.847 36.562 −1.191 1.00 7.00 C ATOM 1273 CG PRO A 172 34.215 37.871 −1.313 1.00 7.00 C ATOM 1274 CD PRO A 172 33.920 38.058 −2.754 1.00 7.00 C ATOM 1275 O PRO A 172 34.581 34.314 −2.813 1.00 7.00 O ATOM 1276 N ASN A 173 36.751 34.443 −3.383 1.00 39.83 N ATOM 1277 CA ASN A 173 36.885 33.048 −3.765 1.00 39.83 C ATOM 1278 C ASN A 173 37.159 32.151 −2.551 1.00 39.83 C ATOM 1279 CB ASN A 173 38.023 32.927 −4.787 1.00 39.83 C ATOM 1280 CG ASN A 173 38.182 31.518 −5.339 1.00 39.83 C ATOM 1281 OD1 ASN A 173 37.393 31.074 −6.174 1.00 39.83 O ATOM 1282 ND2 ASN A 173 39.224 30.816 −4.888 1.00 39.83 N ATOM 1283 O ASN A 173 37.970 31.234 −2.625 1.00 39.83 O ATOM 1284 N LEU A 174 36.469 32.391 −1.438 1.00 9.35 N ATOM 1285 CA LEU A 174 36.856 31.739 −0.194 1.00 9.35 C ATOM 1286 C LEU A 174 35.744 31.028 0.552 1.00 9.35 C ATOM 1287 CB LEU A 174 37.526 32.738 0.745 1.00 9.35 C ATOM 1288 CG LEU A 174 38.918 32.310 1.227 1.00 9.35 C ATOM 1289 CD1 LEU A 174 39.228 32.933 2.575 1.00 9.35 C ATOM 1290 CD2 LEU A 174 39.041 30.792 1.296 1.00 9.35 C ATOM 1291 O LEU A 174 36.012 30.098 1.305 1.00 9.35 O ATOM 1292 N SER A 175 34.506 31.464 0.364 1.00 30.39 N ATOM 1293 CA SER A 175 33.364 30.876 1.082 1.00 30.39 C ATOM 1294 C SER A 175 33.247 31.385 2.527 1.00 30.39 C ATOM 1295 CB SER A 175 33.365 29.338 1.033 1.00 30.39 C ATOM 1296 OG SER A 175 34.053 28.763 2.126 1.00 30.39 O ATOM 1297 O SER A 175 34.242 31.681 3.192 1.00 30.39 O ATOM 1298 N SER A 176 32.015 31.474 3.002 1.00 24.01 N ATOM 1299 CA SER A 176 31.707 32.242 4.196 1.00 24.01 C ATOM 1300 C SER A 176 31.239 31.395 5.367 1.00 24.01 C ATOM 1301 CB SER A 176 30.605 33.250 3.866 1.00 24.01 C ATOM 1302 OG SER A 176 29.537 32.606 3.179 1.00 24.01 O ATOM 1303 O SER A 176 31.974 30.551 5.883 1.00 24.01 O ATOM 1304 N GLY A 177 29.997 31.646 5.772 1.00 45.64 N ATOM 1305 CA GLY A 177 29.411 31.028 6.946 1.00 45.64 C ATOM 1306 C GLY A 177 29.171 29.536 6.832 1.00 45.64 C ATOM 1307 O GLY A 177 28.189 29.107 6.221 1.00 45.64 O ATOM 1308 N PRO A 178 30.077 28.732 7.418 1.00 55.63 N ATOM 1309 CA PRO A 178 29.757 27.315 7.528 1.00 55.63 C ATOM 1310 C PRO A 178 28.416 27.247 8.205 1.00 55.63 C ATOM 1311 CB PRO A 178 30.841 26.776 8.459 1.00 55.63 C ATOM 1312 CG PRO A 178 31.967 27.729 8.317 1.00 55.63 C ATOM 1313 CD PRO A 178 31.333 29.069 8.107 1.00 55.63 C ATOM 1314 O PRO A 178 28.135 28.014 9.129 1.00 55.63 O ATOM 1315 N ILE A 179 27.589 26.334 7.732 1.00 28.13 N ATOM 1316 CA ILE A 179 26.200 26.283 8.129 1.00 28.13 C ATOM 1317 C ILE A 179 26.033 25.850 9.592 1.00 28.13 C ATOM 1318 O ILE A 179 26.689 24.913 10.044 1.00 28.13 O ATOM 1319 CB ILE A 179 25.450 25.346 7.181 1.00 28.13 C ATOM 1320 CG1 ILE A 179 23.986 25.765 7.076 1.00 28.13 C ATOM 1321 CG2 ILE A 179 25.644 23.894 7.592 1.00 28.13 C ATOM 1322 CD1 ILE A 179 23.104 24.748 6.391 1.00 28.13 C ATOM 1323 N ASP A 180 25.186 26.551 10.348 1.00 30.29 N ATOM 1324 CA ASP A 180 24.914 26.099 11.706 1.00 30.29 C ATOM 1325 C ASP A 180 24.251 24.737 11.610 1.00 30.29 C ATOM 1326 O ASP A 180 23.055 24.636 11.348 1.00 30.29 O ATOM 1327 CB ASP A 180 24.015 27.065 12.468 1.00 30.29 C ATOM 1328 CG ASP A 180 23.550 26.490 13.793 1.00 30.29 C ATOM 1329 OD1 ASP A 180 24.216 25.567 14.310 1.00 30.29 O ATOM 1330 OD2 ASP A 180 22.521 26.961 14.320 1.00 30.29 O ATOM 1331 N SER A 181 25.042 23.695 11.824 1.00 27.74 N ATOM 1332 CA SER A 181 24.613 22.322 11.576 1.00 27.74 C ATOM 1333 C SER A 181 23.393 21.889 12.391 1.00 27.74 C ATOM 1334 O SER A 181 22.923 20.751 12.274 1.00 27.74 O ATOM 1335 CB SER A 181 25.777 21.359 11.836 1.00 27.74 C ATOM 1336 OG SER A 181 26.348 21.583 13.117 1.00 27.74 O ATOM 1337 N SER A 182 22.887 22.798 13.217 1.00 49.81 N ATOM 1338 CA SER A 182 21.770 22.491 14.098 1.00 49.81 C ATOM 1339 C SER A 182 20.479 22.398 13.309 1.00 49.81 C ATOM 1340 O SER A 182 19.603 21.595 13.623 1.00 49.81 O ATOM 1341 CB SER A 182 21.636 23.574 15.165 1.00 49.81 C ATOM 1342 OG SER A 182 22.905 23.904 15.704 1.00 49.81 O ATOM 1343 N VAL A 183 20.387 23.215 12.267 1.00 16.03 N ATOM 1344 CA VAL A 183 19.154 23.406 11.519 1.00 16.03 C ATOM 1345 C VAL A 183 18.864 22.287 10.534 1.00 16.03 C ATOM 1346 O VAL A 183 17.926 22.385 9.752 1.00 16.03 O ATOM 1347 CB VAL A 183 19.213 24.715 10.728 1.00 16.03 C ATOM 1348 CG1 VAL A 183 19.853 25.805 11.568 1.00 16.03 C ATOM 1349 CG2 VAL A 183 20.015 24.517 9.467 1.00 16.03 C ATOM 1350 N LEU A 184 19.664 21.228 10.562 1.00 18.29 N ATOM 1351 CA LEU A 184 19.483 20.133 9.621 1.00 18.29 C ATOM 1352 C LEU A 184 18.488 19.111 10.132 1.00 18.29 C ATOM 1353 O LEU A 184 17.488 18.832 9.479 1.00 18.29 O ATOM 1354 CB LEU A 184 20.806 19.432 9.334 1.00 18.29 C ATOM 1355 CG LEU A 184 21.893 20.188 8.579 1.00 18.29 C ATOM 1356 CD1 LEU A 184 22.556 19.254 7.579 1.00 18.29 C ATOM 1357 CD2 LEU A 184 21.310 21.387 7.857 1.00 18.29 C ATOM 1358 N SER A 185 18.777 18.546 11.296 1.00 16.52 N ATOM 1359 CA SER A 185 17.944 17.501 11.869 1.00 16.52 C ATOM 1360 C SER A 185 17.974 17.589 13.387 1.00 16.52 C ATOM 1361 O SER A 185 18.996 17.966 13.968 1.00 16.52 O ATOM 1362 CB SER A 185 18.434 16.131 11.401 1.00 16.52 C ATOM 1363 OG SER A 185 17.922 15.093 12.211 1.00 16.52 O ATOM 1364 N ARG A 186 16.852 17.264 14.025 1.00 9.03 N ATOM 1365 CA ARG A 186 16.807 17.201 15.480 1.00 9.03 C ATOM 1366 C ARG A 186 17.579 15.978 15.991 1.00 9.03 C ATOM 1367 O ARG A 186 17.880 15.863 17.178 1.00 9.03 O ATOM 1368 CB ARG A 186 15.362 17.141 15.954 1.00 9.03 C ATOM 1369 CG ARG A 186 14.541 18.356 15.603 1.00 9.03 C ATOM 1370 CD ARG A 186 13.063 18.164 15.966 1.00 9.03 C ATOM 1371 NE ARG A 186 12.327 17.398 14.955 1.00 9.03 N ATOM 1372 CZ ARG A 186 11.030 17.115 15.019 1.00 9.03 C ATOM 1373 NH1 ARG A 186 10.303 17.521 16.054 1.00 9.03 N ATOM 1374 NH2 ARG A 186 10.460 16.424 14.045 1.00 9.03 N ATOM 1375 N ASN A 187 17.889 15.067 15.073 1.00 5.37 N ATOM 1376 CA ASN A 187 18.609 13.849 15.381 1.00 5.37 C ATOM 1377 C ASN A 187 20.080 14.165 15.499 1.00 5.37 C ATOM 1378 O ASN A 187 20.770 14.280 14.499 1.00 5.37 O ATOM 1379 CB ASN A 187 18.391 12.835 14.261 1.00 5.37 C ATOM 1380 CG ASN A 187 19.085 11.512 14.520 1.00 5.37 C ATOM 1381 OD1 ASN A 187 19.711 11.319 15.557 1.00 5.37 O ATOM 1382 ND2 ASN A 187 18.972 10.590 13.574 1.00 5.37 N ATOM 1383 N LYS A 188 20.562 14.316 16.725 1.00 28.56 N ATOM 1384 CA LYS A 188 21.953 14.680 16.949 1.00 28.56 C ATOM 1385 C LYS A 188 22.890 13.654 16.351 1.00 28.56 C ATOM 1386 O LYS A 188 23.961 13.987 15.871 1.00 28.56 O ATOM 1387 CB LYS A 188 22.232 14.836 18.441 1.00 28.56 C ATOM 1388 CG LYS A 188 21.271 15.774 19.144 1.00 28.56 C ATOM 1389 CD LYS A 188 21.864 16.328 20.434 1.00 28.56 C ATOM 1390 CE LYS A 188 20.791 17.010 21.275 1.00 28.56 C ATOM 1391 NZ LYS A 188 19.790 17.724 20.420 1.00 28.56 N ATOM 1392 N THR A 189 22.473 12.399 16.385 1.00 6.44 N ATOM 1393 CA THR A 189 23.280 11.307 15.860 1.00 6.44 C ATOM 1394 C THR A 189 23.643 11.552 14.403 1.00 6.44 C ATOM 1395 O THR A 189 24.811 11.466 14.031 1.00 6.44 O ATOM 1396 CB THR A 189 22.548 9.948 15.974 1.00 6.44 C ATOM 1397 OG1 THR A 189 22.081 9.747 17.314 1.00 6.44 O ATOM 1398 CG2 THR A 189 23.478 8.815 15.593 1.00 6.44 C ATOM 1399 N GLU A 190 22.638 11.848 13.584 1.00 13.34 N ATOM 1400 CA GLU A 190 22.846 12.130 12.166 1.00 13.34 C ATOM 1401 C GLU A 190 23.514 13.486 11.943 1.00 13.34 C ATOM 1402 O GLU A 190 23.904 13.824 10.826 1.00 13.34 O ATOM 1403 CB GLU A 190 21.517 12.087 11.412 1.00 13.34 C ATOM 1404 CG GLU A 190 20.918 10.707 11.270 1.00 13.34 C ATOM 1405 CD GLU A 190 21.690 9.822 10.303 1.00 13.34 C ATOM 1406 OE1 GLU A 190 22.590 10.332 9.589 1.00 13.34 O ATOM 1407 OE2 GLU A 190 21.388 8.606 10.268 1.00 13.34 O ATOM 1408 N VAL A 191 23.637 14.254 13.018 1.00 19.62 N ATOM 1409 CA VAL A 191 24.253 15.569 12.964 1.00 19.62 C ATOM 1410 C VAL A 191 25.744 15.476 13.210 1.00 19.62 C ATOM 1411 O VAL A 191 26.523 16.213 12.612 1.00 19.62 O ATOM 1412 CB VAL A 191 23.665 16.506 14.012 1.00 19.62 C ATOM 1413 CG1 VAL A 191 24.549 17.726 14.151 1.00 19.62 C ATOM 1414 CG2 VAL A 191 22.259 16.901 13.633 1.00 19.62 C ATOM 1415 N ASP A 192 26.135 14.585 14.113 1.00 25.27 N ATOM 1416 CA ASP A 192 27.537 14.312 14.339 1.00 25.27 C ATOM 1417 C ASP A 192 28.071 13.748 13.057 1.00 25.27 C ATOM 1418 O ASP A 192 29.146 14.123 12.601 1.00 25.27 O ATOM 1419 CB ASP A 192 27.717 13.274 15.432 1.00 25.27 C ATOM 1420 CG ASP A 192 27.232 13.757 16.775 1.00 25.27 C ATOM 1421 OD1 ASP A 192 27.127 14.991 16.956 1.00 25.27 O ATOM 1422 OD2 ASP A 192 26.958 12.900 17.647 1.00 25.27 O ATOM 1423 N ILE A 193 27.305 12.836 12.474 1.00 8.05 N ATOM 1424 CA ILE A 193 27.728 12.182 11.244 1.00 8.05 C ATOM 1425 C ILE A 193 28.014 13.217 10.170 1.00 8.05 C ATOM 1426 O ILE A 193 28.916 13.040 9.361 1.00 8.05 O ATOM 1427 CB ILE A 193 26.657 11.218 10.714 1.00 8.05 C ATOM 1428 CG1 ILE A 193 26.355 10.133 11.738 1.00 8.05 C ATOM 1429 CG2 ILE A 193 27.094 10.605 9.406 1.00 8.05 C ATOM 1430 CD1 ILE A 193 25.020 9.507 11.524 1.00 8.05 C ATOM 1431 N TYR A 194 27.234 14.293 10.159 1.00 8.06 N ATOM 1432 CA TYR A 194 27.461 15.364 9.202 1.00 8.06 C ATOM 1433 C TYR A 194 28.779 16.067 9.488 1.00 8.06 C ATOM 1434 O TYR A 194 29.553 16.324 8.580 1.00 8.06 O ATOM 1435 CB TYR A 194 26.310 16.367 9.208 1.00 8.06 C ATOM 1436 CG TYR A 194 26.491 17.489 8.211 1.00 8.06 C ATOM 1437 CD1 TYR A 194 26.054 17.364 6.915 1.00 8.06 C ATOM 1438 CD2 TYR A 194 27.110 18.679 8.569 1.00 8.06 C ATOM 1439 CE1 TYR A 194 26.219 18.396 6.002 1.00 8.06 C ATOM 1440 CE2 TYR A 194 27.276 19.718 7.654 1.00 8.06 C ATOM 1441 CZ TYR A 194 26.827 19.564 6.376 1.00 8.06 C ATOM 1442 OH TYR A 194 26.991 20.567 5.456 1.00 8.06 O ATOM 1443 N ASN A 195 29.047 16.361 10.751 1.00 8.63 N ATOM 1444 CA ASN A 195 30.263 17.082 11.093 1.00 8.63 C ATOM 1445 C ASN A 195 31.493 16.183 11.160 1.00 8.63 C ATOM 1446 O ASN A 195 32.492 16.553 11.756 1.00 8.63 O ATOM 1447 CB ASN A 195 30.103 17.824 12.424 1.00 8.63 C ATOM 1448 CG ASN A 195 28.853 18.679 12.475 1.00 8.63 C ATOM 1449 OD1 ASN A 195 27.923 18.489 11.693 1.00 8.63 O ATOM 1450 ND2 ASN A 195 28.819 19.622 13.410 1.00 8.63 N ATOM 1451 N SER A 196 31.426 15.005 10.559 1.00 23.86 N ATOM 1452 CA SER A 196 32.503 14.031 10.705 1.00 23.86 C ATOM 1453 C SER A 196 32.876 13.419 9.362 1.00 23.86 C ATOM 1454 O SER A 196 34.017 13.007 9.154 1.00 23.86 O ATOM 1455 CB SER A 196 32.111 12.924 11.697 1.00 23.86 C ATOM 1456 OG SER A 196 31.983 13.408 13.032 1.00 23.86 O ATOM 1457 N ASP A 197 31.914 13.370 8.448 1.00 30.45 N ATOM 1458 CA ASP A 197 32.159 12.836 7.113 1.00 30.45 C ATOM 1459 C ASP A 197 33.080 13.721 6.278 1.00 30.45 C ATOM 1460 O ASP A 197 32.724 14.850 5.937 1.00 30.45 O ATOM 1461 CB ASP A 197 30.848 12.648 6.370 1.00 30.45 C ATOM 1462 CG ASP A 197 31.049 12.455 4.892 1.00 30.45 C ATOM 1463 OD1 ASP A 197 32.144 12.025 4.470 1.00 30.45 O ATOM 1464 OD2 ASP A 197 30.098 12.734 4.148 1.00 30.45 O ATOM 1465 N PRO A 198 34.251 13.186 5.906 1.00 26.01 N ATOM 1466 CA PRO A 198 35.306 13.921 5.192 1.00 26.01 C ATOM 1467 C PRO A 198 34.821 14.622 3.931 1.00 26.01 C ATOM 1468 O PRO A 198 35.365 15.662 3.560 1.00 26.01 O ATOM 1469 CB PRO A 198 36.293 12.825 4.799 1.00 26.01 C ATOM 1470 CG PRO A 198 36.040 11.724 5.767 1.00 26.01 C ATOM 1471 CD PRO A 198 34.586 11.767 6.095 1.00 26.01 C ATOM 1472 N LEU A 199 33.805 14.062 3.289 1.00 23.23 N ATOM 1473 CA LEU A 199 33.445 14.479 1.943 1.00 23.23 C ATOM 1474 C LEU A 199 32.470 15.646 1.860 1.00 23.23 C ATOM 1475 O LEU A 199 32.145 16.097 0.761 1.00 23.23 O ATOM 1476 CB LEU A 199 32.890 13.297 1.153 1.00 23.23 C ATOM 1477 CG LEU A 199 33.781 12.061 1.040 1.00 23.23 C ATOM 1478 CD1 LEU A 199 33.061 10.986 0.231 1.00 23.23 C ATOM 1479 CD2 LEU A 199 35.139 12.398 0.437 1.00 23.23 C ATOM 1480 N ILE A 200 31.996 16.140 3.000 1.00 17.69 N ATOM 1481 CA ILE A 200 31.094 17.288 2.963 1.00 17.69 C ATOM 1482 C ILE A 200 31.839 18.578 3.137 1.00 17.69 C ATOM 1483 O ILE A 200 32.525 18.760 4.128 1.00 17.69 O ATOM 1484 CB ILE A 200 29.994 17.226 4.033 1.00 17.69 C ATOM 1485 CG1 ILE A 200 30.194 16.019 4.932 1.00 17.69 C ATOM 1486 CG2 ILE A 200 28.643 17.112 3.388 1.00 17.69 C ATOM 1487 CD1 ILE A 200 28.882 15.439 5.427 1.00 17.69 C ATOM 1488 N CYS A 201 31.706 19.486 2.182 1.00 8.66 N ATOM 1489 CA CYS A 201 32.262 20.809 2.400 1.00 8.66 C ATOM 1490 C CYS A 201 31.423 21.505 3.455 1.00 8.66 C ATOM 1491 O CYS A 201 30.288 21.898 3.202 1.00 8.66 O ATOM 1492 CB CYS A 201 32.297 21.638 1.115 1.00 8.66 C ATOM 1493 SG CYS A 201 33.139 23.245 1.295 1.00 8.66 S ATOM 1494 N ARG A 202 31.969 21.649 4.651 1.00 11.88 N ATOM 1495 CA ARG A 202 31.221 22.298 5.719 1.00 11.88 C ATOM 1496 C ARG A 202 31.371 23.819 5.672 1.00 11.88 C ATOM 1497 O ARG A 202 30.593 24.557 6.283 1.00 11.88 O ATOM 1498 CB ARG A 202 31.657 21.767 7.078 1.00 11.88 C ATOM 1499 CG ARG A 202 31.099 20.419 7.430 1.00 11.88 C ATOM 1500 CD ARG A 202 31.887 19.875 8.577 1.00 11.88 C ATOM 1501 NE ARG A 202 31.791 18.426 8.653 1.00 11.88 N ATOM 1502 CZ ARG A 202 32.354 17.576 7.800 1.00 11.88 C ATOM 1503 NH1 ARG A 202 33.054 18.014 6.763 1.00 11.88 N ATOM 1504 NH2 ARG A 202 32.198 16.273 7.988 1.00 11.88 N ATOM 1505 N ALA A 203 32.387 24.277 4.953 1.00 56.18 N ATOM 1506 CA ALA A 203 32.568 25.699 4.719 1.00 56.18 C ATOM 1507 C ALA A 203 31.276 26.274 4.189 1.00 56.18 C ATOM 1508 O ALA A 203 30.490 25.566 3.550 1.00 56.18 O ATOM 1509 CB ALA A 203 33.670 25.923 3.714 1.00 56.18 C ATOM 1510 N GLY A 204 31.054 27.556 4.451 1.00 47.62 N ATOM 1511 CA GLY A 204 29.916 28.241 3.876 1.00 47.62 C ATOM 1512 C GLY A 204 30.014 28.153 2.369 1.00 47.62 C ATOM 1513 O GLY A 204 30.369 27.109 1.814 1.00 47.62 O ATOM 1514 N LEU A 205 29.724 29.250 1.685 1.00 35.86 N ATOM 1515 CA LEU A 205 29.826 29.200 0.239 1.00 35.86 C ATOM 1516 C LEU A 205 30.419 30.433 −0.422 1.00 35.86 C ATOM 1517 O LEU A 205 30.219 31.564 0.019 1.00 35.86 O ATOM 1518 CB LEU A 205 28.486 28.843 −0.383 1.00 35.86 C ATOM 1519 CG LEU A 205 28.597 28.516 −1.866 1.00 35.86 C ATOM 1520 CD1 LEU A 205 29.781 27.583 −2.174 1.00 35.86 C ATOM 1521 CD2 LEU A 205 27.270 27.939 −2.326 1.00 35.86 C ATOM 1522 N LYS A 206 31.161 30.164 −1.490 1.00 34.06 N ATOM 1523 CA LYS A 206 31.799 31.171 −2.308 1.00 34.06 C ATOM 1524 C LYS A 206 30.738 32.080 −2.921 1.00 34.06 C ATOM 1525 O LYS A 206 29.543 31.829 −2.788 1.00 34.06 O ATOM 1526 CB LYS A 206 32.603 30.484 −3.415 1.00 34.06 C ATOM 1527 CG LYS A 206 33.630 29.452 −2.936 1.00 34.06 C ATOM 1528 CD LYS A 206 35.024 30.063 −2.795 1.00 34.06 C ATOM 1529 CE LYS A 206 36.133 29.001 −2.724 1.00 34.06 C ATOM 1530 NZ LYS A 206 36.574 28.630 −1.336 1.00 34.06 N ATOM 1531 N VAL A 207 31.169 33.132 −3.604 1.00 31.59 N ATOM 1532 CA VAL A 207 30.211 34.061 −4.168 1.00 31.59 C ATOM 1533 C VAL A 207 29.919 33.748 −5.636 1.00 31.59 C ATOM 1534 O VAL A 207 28.990 34.302 −6.222 1.00 31.59 O ATOM 1535 CB VAL A 207 30.662 35.514 −3.967 1.00 31.59 C ATOM 1536 CG1 VAL A 207 29.538 36.482 −4.318 1.00 31.59 C ATOM 1537 CG2 VAL A 207 31.094 35.713 −2.527 1.00 31.59 C ATOM 1538 N CYS A 208 30.691 32.839 −6.222 1.00 43.48 N ATOM 1539 CA CYS A 208 30.434 32.411 −7.599 1.00 43.48 C ATOM 1540 C CYS A 208 29.399 31.287 −7.669 1.00 43.48 C ATOM 1541 O CYS A 208 29.078 30.786 −8.753 1.00 43.48 O ATOM 1542 CB CYS A 208 31.731 31.982 −8.298 1.00 43.48 C ATOM 1543 SG CYS A 208 32.724 30.771 −7.393 1.00 43.48 S ATOM 1544 N PHE A 209 28.874 30.899 −6.510 1.00 4.14 N ATOM 1545 CA PHE A 209 27.976 29.761 −6.446 1.00 4.14 C ATOM 1546 C PHE A 209 26.626 30.153 −5.868 1.00 4.14 C ATOM 1547 O PHE A 209 25.584 29.628 −6.279 1.00 4.14 O ATOM 1548 CB PHE A 209 28.606 28.651 −5.620 1.00 4.14 C ATOM 1549 CG PHE A 209 28.071 27.291 −5.932 1.00 4.14 C ATOM 1550 CD1 PHE A 209 28.261 26.735 −7.179 1.00 4.14 C ATOM 1551 CD2 PHE A 209 27.383 26.561 −4.975 1.00 4.14 C ATOM 1552 CE1 PHE A 209 27.759 25.481 −7.457 1.00 4.14 C ATOM 1553 CE2 PHE A 209 26.896 25.304 −5.248 1.00 4.14 C ATOM 1554 CZ PHE A 209 27.078 24.766 −6.485 1.00 4.14 C ATOM 1555 N GLY A 210 26.642 31.085 −4.919 1.00 25.31 N ATOM 1556 CA GLY A 210 25.409 31.653 −4.409 1.00 25.31 C ATOM 1557 C GLY A 210 24.554 32.112 −5.577 1.00 25.31 C ATOM 1558 O GLY A 210 23.354 31.853 −5.620 1.00 25.31 O ATOM 1559 N ILE A 211 25.193 32.786 −6.531 1.00 18.65 N ATOM 1560 CA ILE A 211 24.555 33.223 −7.770 1.00 18.65 C ATOM 1561 C ILE A 211 23.916 32.087 −8.565 1.00 18.65 C ATOM 1562 O ILE A 211 22.767 32.188 −8.992 1.00 18.65 O ATOM 1563 CB ILE A 211 25.569 33.923 −8.676 1.00 18.65 C ATOM 1564 CG1 ILE A 211 26.141 35.147 −7.964 1.00 18.65 C ATOM 1565 CG2 ILE A 211 24.927 34.296 −10.011 1.00 18.65 C ATOM 1566 CD1 ILE A 211 27.434 35.622 −8.548 1.00 18.65 C ATOM 1567 N GLN A 212 24.660 31.007 −8.774 1.00 5.98 N ATOM 1568 CA GLN A 212 24.116 29.864 −9.504 1.00 5.98 C ATOM 1569 C GLN A 212 22.999 29.180 −8.734 1.00 5.98 C ATOM 1570 O GLN A 212 22.254 28.388 −9.286 1.00 5.98 O ATOM 1571 CB GLN A 212 25.216 28.878 −9.894 1.00 5.98 C ATOM 1572 CG GLN A 212 26.201 29.454 −10.915 1.00 5.98 C ATOM 1573 CD GLN A 212 25.589 29.645 −12.286 1.00 5.98 C ATOM 1574 OE1 GLN A 212 24.430 29.305 −12.514 1.00 5.98 O ATOM 1575 NE2 GLN A 212 26.369 30.183 −13.212 1.00 5.98 N ATOM 1576 N LEU A 213 22.885 29.513 −7.457 1.00 29.72 N ATOM 1577 CA LEU A 213 21.757 29.081 −6.657 1.00 29.72 C ATOM 1578 C LEU A 213 20.658 30.139 −6.662 1.00 29.72 C ATOM 1579 O LEU A 213 19.564 29.915 −6.139 1.00 29.72 O ATOM 1580 CB LEU A 213 22.196 28.783 −5.230 1.00 29.72 C ATOM 1581 CG LEU A 213 22.983 27.484 −5.094 1.00 29.72 C ATOM 1582 CD1 LEU A 213 22.926 26.972 −3.670 1.00 29.72 C ATOM 1583 CD2 LEU A 213 22.438 26.443 −6.045 1.00 29.72 C ATOM 1584 N LEU A 214 20.954 31.301 −7.236 1.00 8.58 N ATOM 1585 CA LEU A 214 19.913 32.272 −7.530 1.00 8.58 C ATOM 1586 C LEU A 214 19.426 32.015 −8.938 1.00 8.58 C ATOM 1587 O LEU A 214 18.265 32.261 −9.255 1.00 8.58 O ATOM 1588 CB LEU A 214 20.431 33.697 −7.392 1.00 8.58 C ATOM 1589 CG LEU A 214 20.571 34.138 −5.943 1.00 8.58 C ATOM 1590 CD1 LEU A 214 20.723 35.645 −5.877 1.00 8.58 C ATOM 1591 CD2 LEU A 214 19.358 33.676 −5.156 1.00 8.58 C ATOM 1592 N ASN A 215 20.328 31.503 −9.770 1.00 29.13 N ATOM 1593 CA ASN A 215 19.965 31.052 −11.102 1.00 29.13 C ATOM 1594 C ASN A 215 19.301 29.713 −11.024 1.00 29.13 C ATOM 1595 O ASN A 215 18.836 29.184 −12.018 1.00 29.13 O ATOM 1596 CB ASN A 215 21.182 30.950 −12.012 1.00 29.13 C ATOM 1597 CG ASN A 215 21.348 32.170 −12.887 1.00 29.13 C ATOM 1598 OD1 ASN A 215 21.176 33.299 −12.427 1.00 29.13 O ATOM 1599 ND2 ASN A 215 21.666 31.954 −14.160 1.00 29.13 N ATOM 1600 N ALA A 216 19.270 29.165 −9.824 1.00 13.41 N ATOM 1601 CA ALA A 216 18.660 27.876 −9.602 1.00 13.41 C ATOM 1602 C ALA A 216 17.188 28.092 −9.349 1.00 13.41 C ATOM 1603 O ALA A 216 16.335 27.528 −10.031 1.00 13.41 O ATOM 1604 CB ALA A 216 19.298 27.205 −8.427 1.00 13.41 C ATOM 1605 N VAL A 217 16.892 28.931 −8.365 1.00 5.49 N ATOM 1606 CA VAL A 217 15.512 29.202 −7.995 1.00 5.49 C ATOM 1607 C VAL A 217 14.725 29.755 −9.186 1.00 5.49 C ATOM 1608 O VAL A 217 13.687 29.206 −9.573 1.00 5.49 O ATOM 1609 CB VAL A 217 15.452 30.190 −6.840 1.00 5.49 C ATOM 1610 CG1 VAL A 217 14.076 30.174 −6.220 1.00 5.49 C ATOM 1611 CG2 VAL A 217 16.512 29.841 −5.817 1.00 5.49 C ATOM 1612 N SER A 218 15.238 30.838 −9.767 1.00 8.30 N ATOM 1613 CA SER A 218 14.589 31.499 −10.891 1.00 8.30 C ATOM 1614 C SER A 218 14.185 30.496 −11.951 1.00 8.30 C ATOM 1615 O SER A 218 13.041 30.492 −12.406 1.00 8.30 O ATOM 1616 CB SER A 218 15.535 32.502 −11.514 1.00 8.30 C ATOM 1617 OG SER A 218 16.740 31.849 −11.825 1.00 8.30 O ATOM 1618 N ARG A 219 15.131 29.649 −12.347 1.00 7.64 N ATOM 1619 CA ARG A 219 14.877 28.661 −13.383 1.00 7.64 C ATOM 1620 C ARG A 219 13.801 27.686 −12.954 1.00 7.64 C ATOM 1621 O ARG A 219 13.011 27.236 −13.771 1.00 7.64 O ATOM 1622 CB ARG A 219 16.148 27.902 −13.738 1.00 7.64 C ATOM 1623 CG ARG A 219 17.168 28.737 −14.476 1.00 7.64 C ATOM 1624 CD ARG A 219 18.477 27.981 −14.687 1.00 7.64 C ATOM 1625 NE ARG A 219 19.557 28.891 −15.061 1.00 7.64 N ATOM 1626 CZ ARG A 219 20.779 28.508 −15.406 1.00 7.64 C ATOM 1627 NH1 ARG A 219 21.091 27.214 −15.427 1.00 7.64 N ATOM 1628 NH2 ARG A 219 21.684 29.422 −15.733 1.00 7.64 N ATOM 1629 N VAL A 220 13.774 27.352 −11.671 1.00 30.77 N ATOM 1630 CA VAL A 220 12.777 26.421 −11.159 1.00 30.77 C ATOM 1631 C VAL A 220 11.399 27.088 −11.136 1.00 30.77 C ATOM 1632 O VAL A 220 10.383 26.450 −11.416 1.00 30.77 O ATOM 1633 CB VAL A 220 13.157 25.907 −9.751 1.00 30.77 C ATOM 1634 CG1 VAL A 220 12.127 24.932 −9.242 1.00 30.77 C ATOM 1635 CG2 VAL A 220 14.511 25.242 −9.777 1.00 30.77 C ATOM 1636 N GLU A 221 11.378 28.379 −10.821 1.00 27.47 N ATOM 1637 CA GLU A 221 10.140 29.150 −10.793 1.00 27.47 C ATOM 1638 C GLU A 221 9.477 29.216 −12.170 1.00 27.47 C ATOM 1639 O GLU A 221 8.255 29.244 −12.282 1.00 27.47 O ATOM 1640 CB GLU A 221 10.412 30.556 −10.251 1.00 27.47 C ATOM 1641 CG GLU A 221 9.181 31.441 −10.165 1.00 27.47 C ATOM 1642 CD GLU A 221 9.353 32.595 −9.198 1.00 27.47 C ATOM 1643 OE1 GLU A 221 9.613 33.738 −9.646 1.00 27.47 O ATOM 1644 OE2 GLU A 221 9.233 32.355 −7.983 1.00 27.47 O ATOM 1645 N ARG A 222 10.282 29.236 −13.221 1.00 27.30 N ATOM 1646 CA ARG A 222 9.732 29.188 −14.564 1.00 27.30 C ATOM 1647 C ARG A 222 9.348 27.761 −14.911 1.00 27.30 C ATOM 1648 O ARG A 222 8.552 27.526 −15.815 1.00 27.30 O ATOM 1649 CB ARG A 222 10.742 29.696 −15.592 1.00 27.30 C ATOM 1650 CG ARG A 222 11.007 31.186 −15.540 1.00 27.30 C ATOM 1651 CD ARG A 222 11.646 31.682 −16.830 1.00 27.30 C ATOM 1652 NE ARG A 222 12.799 30.885 −17.263 1.00 27.30 N ATOM 1653 CZ ARG A 222 14.042 31.014 −16.791 1.00 27.30 C ATOM 1654 NH1 ARG A 222 14.310 31.909 −15.846 1.00 27.30 N ATOM 1655 NH2 ARG A 222 15.020 30.241 −17.261 1.00 27.30 N ATOM 1656 N ALA A 223 9.923 26.811 −14.184 1.00 20.16 N ATOM 1657 CA ALA A 223 9.854 25.402 −14.549 1.00 20.16 C ATOM 1658 C ALA A 223 8.603 24.694 −14.033 1.00 20.16 C ATOM 1659 O ALA A 223 8.067 23.808 −14.691 1.00 20.16 O ATOM 1660 CB ALA A 223 11.101 24.688 −14.068 1.00 20.16 C ATOM 1661 N LEU A 224 8.135 25.084 −12.858 1.00 25.21 N ATOM 1662 CA LEU A 224 6.992 24.423 −12.239 1.00 25.21 C ATOM 1663 C LEU A 224 5.784 24.191 −13.145 1.00 25.21 C ATOM 1664 O LEU A 224 5.219 23.105 −13.132 1.00 25.21 O ATOM 1665 CB LEU A 224 6.550 25.193 −11.006 1.00 25.21 C ATOM 1666 CG LEU A 224 7.686 25.484 −10.033 1.00 25.21 C ATOM 1667 CD1 LEU A 224 7.306 26.655 −9.127 1.00 25.21 C ATOM 1668 CD2 LEU A 224 8.050 24.236 −9.228 1.00 25.21 C ATOM 1669 N PRO A 225 5.370 25.210 −13.921 1.00 34.97 N ATOM 1670 CA PRO A 225 4.116 25.093 −14.677 1.00 34.97 C ATOM 1671 C PRO A 225 4.185 24.008 −15.735 1.00 34.97 C ATOM 1672 O PRO A 225 3.188 23.362 −16.047 1.00 34.97 O ATOM 1673 CB PRO A 225 3.991 26.458 −15.359 1.00 34.97 C ATOM 1674 CG PRO A 225 4.850 27.366 −14.566 1.00 34.97 C ATOM 1675 CD PRO A 225 6.000 26.524 −14.122 1.00 34.97 C ATOM 1676 N LYS A 226 5.372 23.817 −16.285 1.00 58.40 N ATOM 1677 CA LYS A 226 5.564 22.875 −17.364 1.00 58.40 C ATOM 1678 C LYS A 226 5.805 21.485 −16.798 1.00 58.40 C ATOM 1679 O LYS A 226 6.261 20.586 −17.500 1.00 58.40 O ATOM 1680 CB LYS A 226 6.733 23.338 −18.233 1.00 58.40 C ATOM 1681 CG LYS A 226 6.664 24.835 −18.563 1.00 58.40 C ATOM 1682 CD LYS A 226 7.572 25.247 −19.721 1.00 58.40 C ATOM 1683 CE LYS A 226 6.936 26.395 −20.508 1.00 58.40 C ATOM 1684 NZ LYS A 226 7.876 27.086 −21.444 1.00 58.40 N ATOM 1685 N LEU A 227 5.488 21.311 −15.519 1.00 11.13 N ATOM 1686 CA LEU A 227 5.699 20.031 −14.859 1.00 11.13 C ATOM 1687 C LEU A 227 4.512 19.107 −15.015 1.00 11.13 C ATOM 1688 O LEU A 227 3.409 19.406 −14.571 1.00 11.13 O ATOM 1689 CB LEU A 227 6.006 20.225 −13.381 1.00 11.13 C ATOM 1690 CG LEU A 227 7.456 20.544 −13.054 1.00 11.13 C ATOM 1691 CD1 LEU A 227 7.598 20.624 −11.563 1.00 11.13 C ATOM 1692 CD2 LEU A 227 8.362 19.473 −13.600 1.00 11.13 C ATOM 1693 N THR A 228 4.761 17.960 −15.628 1.00 19.77 N ATOM 1694 CA THR A 228 3.710 16.992 −15.892 1.00 19.77 C ATOM 1695 C THR A 228 3.967 15.693 −15.147 1.00 19.77 C ATOM 1696 O THR A 228 3.064 14.884 −14.950 1.00 19.77 O ATOM 1697 CB THR A 228 3.657 16.688 −17.387 1.00 19.77 C ATOM 1698 OG1 THR A 228 4.779 15.871 −17.747 1.00 19.77 O ATOM 1699 CG2 THR A 228 3.702 17.990 −18.172 1.00 19.77 C ATOM 1700 N VAL A 229 5.211 15.515 −14.729 1.00 32.12 N ATOM 1701 CA VAL A 229 5.683 14.259 −14.178 1.00 32.12 C ATOM 1702 C VAL A 229 5.098 14.000 −12.798 1.00 32.12 C ATOM 1703 O VAL A 229 5.020 14.911 −11.974 1.00 32.12 O ATOM 1704 CB VAL A 229 7.216 14.274 −14.088 1.00 32.12 C ATOM 1705 CG1 VAL A 229 7.682 15.494 −13.299 1.00 32.12 C ATOM 1706 CG2 VAL A 229 7.743 12.990 −13.474 1.00 32.12 C ATOM 1707 N PRO A 230 4.687 12.748 −12.542 1.00 28.38 N ATOM 1708 CA PRO A 230 4.183 12.337 −11.229 1.00 28.38 C ATOM 1709 C PRO A 230 5.254 12.581 −10.187 1.00 28.38 C ATOM 1710 O PRO A 230 6.408 12.237 −10.457 1.00 28.38 O ATOM 1711 CB PRO A 230 4.013 10.828 −11.379 1.00 28.38 C ATOM 1712 CG PRO A 230 3.948 10.584 −12.827 1.00 28.38 C ATOM 1713 CD PRO A 230 4.772 11.620 −13.482 1.00 28.38 C ATOM 1714 N PHE A 231 4.907 13.145 −9.033 1.00 4.78 N ATOM 1715 CA PHE A 231 5.888 13.227 −7.958 1.00 4.78 C ATOM 1716 C PHE A 231 5.294 13.013 −6.590 1.00 4.78 C ATOM 1717 O PHE A 231 4.104 13.222 −6.384 1.00 4.78 O ATOM 1718 CB PHE A 231 6.667 14.543 −8.001 1.00 4.78 C ATOM 1719 CG PHE A 231 5.824 15.759 −7.792 1.00 4.78 C ATOM 1720 CD1 PHE A 231 5.762 16.367 −6.553 1.00 4.78 C ATOM 1721 CD2 PHE A 231 5.107 16.306 −8.834 1.00 4.78 C ATOM 1722 CE1 PHE A 231 4.994 17.477 −6.361 1.00 4.78 C ATOM 1723 CE2 PHE A 231 4.338 17.422 −8.639 1.00 4.78 C ATOM 1724 CZ PHE A 231 4.285 18.004 −7.404 1.00 4.78 C ATOM 1725 N LEU A 232 6.135 12.563 −5.666 1.00 4.99 N ATOM 1726 CA LEU A 232 5.797 12.483 −4.251 1.00 4.99 C ATOM 1727 C LEU A 232 6.703 13.487 −3.585 1.00 4.99 C ATOM 1728 O LEU A 232 7.884 13.569 −3.930 1.00 4.99 O ATOM 1729 CB LEU A 232 6.068 11.084 −3.690 1.00 4.99 C ATOM 1730 CG LEU A 232 6.446 10.947 −2.205 1.00 4.99 C ATOM 1731 CD1 LEU A 232 5.296 11.269 −1.279 1.00 4.99 C ATOM 1732 CD2 LEU A 232 6.970 9.557 −1.893 1.00 4.99 C ATOM 1733 N LEU A 233 6.157 14.255 −2.643 1.00 7.29 N ATOM 1734 CA LEU A 233 6.885 15.379 −2.080 1.00 7.29 C ATOM 1735 C LEU A 233 6.784 15.436 −0.563 1.00 7.29 C ATOM 1736 O LEU A 233 5.711 15.686 −0.020 1.00 7.29 O ATOM 1737 CB LEU A 233 6.379 16.679 −2.700 1.00 7.29 C ATOM 1738 CG LEU A 233 6.860 17.992 −2.080 1.00 7.29 C ATOM 1739 CD1 LEU A 233 8.336 18.170 −2.314 1.00 7.29 C ATOM 1740 CD2 LEU A 233 6.091 19.176 −2.644 1.00 7.29 C ATOM 1741 N LEU A 234 7.914 15.215 0.108 1.00 4.78 N ATOM 1742 CA LEU A 234 7.991 15.244 1.566 1.00 4.78 C ATOM 1743 C LEU A 234 8.748 16.489 1.989 1.00 4.78 C ATOM 1744 O LEU A 234 9.688 16.891 1.327 1.00 4.78 O ATOM 1745 CB LEU A 234 8.699 13.994 2.094 1.00 4.78 C ATOM 1746 CG LEU A 234 8.317 12.654 1.458 1.00 4.78 C ATOM 1747 CD1 LEU A 234 9.169 11.532 1.992 1.00 4.78 C ATOM 1748 CD2 LEU A 234 6.848 12.354 1.681 1.00 4.78 C ATOM 1749 N GLN A 235 8.340 17.091 3.097 1.00 4.64 N ATOM 1750 CA GLN A 235 8.813 18.416 3.472 1.00 4.64 C ATOM 1751 C GLN A 235 8.583 18.709 4.952 1.00 4.64 C ATOM 1752 O GLN A 235 7.448 18.703 5.419 1.00 4.64 O ATOM 1753 CB GLN A 235 8.099 19.469 2.620 1.00 4.64 C ATOM 1754 CG GLN A 235 8.183 20.894 3.148 1.00 4.64 C ATOM 1755 CD GLN A 235 9.547 21.510 2.955 1.00 4.64 C ATOM 1756 OE1 GLN A 235 10.239 21.203 1.983 1.00 4.64 O ATOM 1757 NE2 GLN A 235 9.939 22.392 3.871 1.00 4.64 N ATOM 1758 N GLY A 236 9.655 18.973 5.692 1.00 20.71 N ATOM 1759 CA GLY A 236 9.521 19.304 7.099 1.00 20.71 C ATOM 1760 C GLY A 236 8.897 20.668 7.330 1.00 20.71 C ATOM 1761 O GLY A 236 9.211 21.639 6.637 1.00 20.71 O ATOM 1762 N SER A 237 8.008 20.742 8.312 1.00 7.49 N ATOM 1763 CA SER A 237 7.414 22.011 8.723 1.00 7.49 C ATOM 1764 C SER A 237 8.452 23.067 9.099 1.00 7.49 C ATOM 1765 O SER A 237 8.338 24.212 8.697 1.00 7.49 O ATOM 1766 CB SER A 237 6.478 21.787 9.902 1.00 7.49 C ATOM 1767 OG SER A 237 6.289 22.986 10.637 1.00 7.49 O ATOM 1768 N ALA A 238 9.461 22.659 9.865 1.00 5.77 N ATOM 1769 CA ALA A 238 10.473 23.561 10.418 1.00 5.77 C ATOM 1770 C ALA A 238 11.794 23.528 9.648 1.00 5.77 C ATOM 1771 O ALA A 238 12.832 23.154 10.185 1.00 5.77 O ATOM 1772 CB ALA A 238 10.717 23.222 11.884 1.00 5.77 C ATOM 1773 N ASP A 239 11.744 23.952 8.395 1.00 7.96 N ATOM 1774 CA ASP A 239 12.884 23.865 7.491 1.00 7.96 C ATOM 1775 C ASP A 239 13.547 25.227 7.255 1.00 7.96 C ATOM 1776 O ASP A 239 13.090 26.036 6.440 1.00 7.96 O ATOM 1777 CB ASP A 239 12.426 23.255 6.168 1.00 7.96 C ATOM 1778 CG ASP A 239 13.550 22.615 5.398 1.00 7.96 C ATOM 1779 OD1 ASP A 239 14.728 22.918 5.680 1.00 7.96 O ATOM 1780 OD2 ASP A 239 13.245 21.806 4.501 1.00 7.96 O ATOM 1781 N ARG A 240 14.639 25.461 7.975 1.00 53.24 N ATOM 1782 CA ARG A 240 15.357 26.727 7.917 1.00 53.24 C ATOM 1783 C ARG A 240 16.205 26.853 6.658 1.00 53.24 C ATOM 1784 O ARG A 240 16.882 27.852 6.464 1.00 53.24 O ATOM 1785 CB ARG A 240 16.259 26.872 9.145 1.00 53.24 C ATOM 1786 CG ARG A 240 15.534 26.785 10.483 1.00 53.24 C ATOM 1787 CD ARG A 240 15.052 28.156 10.940 1.00 53.24 C ATOM 1788 NE ARG A 240 16.139 29.132 10.928 1.00 53.24 N ATOM 1789 CZ ARG A 240 16.014 30.404 11.291 1.00 53.24 C ATOM 1790 NH1 ARG A 240 14.843 30.869 11.703 1.00 53.24 N ATOM 1791 NH2 ARG A 240 17.065 31.211 11.240 1.00 53.24 N ATOM 1792 N LEU A 241 16.191 25.833 5.812 1.00 6.21 N ATOM 1793 CA LEU A 241 16.954 25.879 4.572 1.00 6.21 C ATOM 1794 C LEU A 241 16.037 26.056 3.376 1.00 6.21 C ATOM 1795 O LEU A 241 15.805 27.166 2.924 1.00 6.21 O ATOM 1796 CB LEU A 241 17.799 24.626 4.418 1.00 6.21 C ATOM 1797 CG LEU A 241 19.264 24.864 4.765 1.00 6.21 C ATOM 1798 CD1 LEU A 241 19.394 26.048 5.667 1.00 6.21 C ATOM 1799 CD2 LEU A 241 19.882 23.636 5.419 1.00 6.21 C ATOM 1800 N CYS A 242 15.515 24.956 2.859 1.00 8.63 N ATOM 1801 CA CYS A 242 14.458 25.044 1.875 1.00 8.63 C ATOM 1802 C CYS A 242 13.172 25.429 2.585 1.00 8.63 C ATOM 1803 O CYS A 242 12.644 24.676 3.386 1.00 8.63 O ATOM 1804 CB CYS A 242 14.308 23.714 1.148 1.00 8.63 C ATOM 1805 SG CYS A 242 15.853 23.207 0.421 1.00 8.63 S ATOM 1806 N ASP A 243 12.694 26.630 2.317 1.00 4.33 N ATOM 1807 CA ASP A 243 11.421 27.078 2.851 1.00 4.33 C ATOM 1808 C ASP A 243 10.359 26.109 2.380 1.00 4.33 C ATOM 1809 O ASP A 243 10.369 25.690 1.222 1.00 4.33 O ATOM 1810 CB ASP A 243 11.106 28.496 2.352 1.00 4.33 C ATOM 1811 CG ASP A 243 9.988 29.148 3.122 1.00 4.33 C ATOM 1812 OD1 ASP A 243 9.635 30.292 2.806 1.00 4.33 O ATOM 1813 OD2 ASP A 243 9.462 28.517 4.054 1.00 4.33 O ATOM 1814 N SER A 244 9.457 25.740 3.282 1.00 10.19 N ATOM 1815 CA SER A 244 8.369 24.840 2.939 1.00 10.19 C ATOM 1816 C SER A 244 7.256 25.577 2.196 1.00 10.19 C ATOM 1817 O SER A 244 6.366 24.956 1.635 1.00 10.19 O ATOM 1818 CB SER A 244 7.805 24.186 4.189 1.00 10.19 C ATOM 1819 OG SER A 244 6.912 25.066 4.836 1.00 10.19 O ATOM 1820 N LYS A 245 7.296 26.901 2.186 1.00 12.84 N ATOM 1821 CA LYS A 245 6.342 27.637 1.375 1.00 12.84 C ATOM 1822 C LYS A 245 6.529 27.248 −0.083 1.00 12.84 C ATOM 1823 O LYS A 245 5.602 27.346 −0.887 1.00 12.84 O ATOM 1824 CB LYS A 245 6.535 29.141 1.538 1.00 12.84 C ATOM 1825 CG LYS A 245 5.425 29.978 0.908 1.00 12.84 C ATOM 1826 CD LYS A 245 5.649 31.481 1.127 1.00 12.84 C ATOM 1827 CE LYS A 245 4.426 32.309 0.715 1.00 12.84 C ATOM 1828 NZ LYS A 245 4.522 33.719 1.214 1.00 12.84 N ATOM 1829 N GLY A 246 7.737 26.802 −0.412 1.00 5.64 N ATOM 1830 CA GLY A 246 8.084 26.418 −1.768 1.00 5.64 C ATOM 1831 C GLY A 246 7.413 25.121 −2.158 1.00 5.64 C ATOM 1832 O GLY A 246 7.008 24.944 −3.303 1.00 5.64 O ATOM 1833 N ALA A 247 7.294 24.214 −1.192 1.00 4.75 N ATOM 1834 CA ALA A 247 6.677 22.920 −1.418 1.00 4.75 C ATOM 1835 C ALA A 247 5.243 23.095 −1.893 1.00 4.75 C ATOM 1836 O ALA A 247 4.805 22.456 −2.849 1.00 4.75 O ATOM 1837 CB ALA A 247 6.720 22.100 −0.155 1.00 4.75 C ATOM 1838 N TYR A 248 4.513 23.976 −1.228 1.00 7.95 N ATOM 1839 CA TYR A 248 3.145 24.265 −1.612 1.00 7.95 C ATOM 1840 C TYR A 248 3.060 24.843 −3.029 1.00 7.95 C ATOM 1841 O TYR A 248 2.119 24.565 −3.779 1.00 7.95 O ATOM 1842 CB TYR A 248 2.527 25.223 −0.595 1.00 7.95 C ATOM 1843 CG TYR A 248 2.496 24.665 0.804 1.00 7.95 C ATOM 1844 CD1 TYR A 248 1.582 23.691 1.159 1.00 7.95 C ATOM 1845 CD2 TYR A 248 3.375 25.113 1.774 1.00 7.95 C ATOM 1846 CE1 TYR A 248 1.538 23.176 2.443 1.00 7.95 C ATOM 1847 CE2 TYR A 248 3.344 24.598 3.060 1.00 7.95 C ATOM 1848 CZ TYR A 248 2.421 23.630 3.385 1.00 7.95 C ATOM 1849 OH TYR A 248 2.383 23.118 4.656 1.00 7.95 O ATOM 1850 N LEU A 249 4.042 25.656 −3.392 1.00 5.59 N ATOM 1851 CA LEU A 249 4.041 26.285 −4.698 1.00 5.59 C ATOM 1852 C LEU A 249 4.162 25.215 −5.737 1.00 5.59 C ATOM 1853 O LEU A 249 3.484 25.240 −6.745 1.00 5.59 O ATOM 1854 CB LEU A 249 5.230 27.215 −4.826 1.00 5.59 C ATOM 1855 CG LEU A 249 4.972 28.509 −5.585 1.00 5.59 C ATOM 1856 CD1 LEU A 249 4.238 29.496 −4.678 1.00 5.59 C ATOM 1857 CD2 LEU A 249 6.300 29.064 −6.044 1.00 5.59 C ATOM 1858 N LEU A 250 5.045 24.268 −5.466 1.00 13.57 N ATOM 1859 CA LEU A 250 5.265 23.130 −6.340 1.00 13.57 C ATOM 1860 C LEU A 250 3.992 22.324 −6.517 1.00 13.57 C ATOM 1861 O LEU A 250 3.660 21.935 −7.630 1.00 13.57 O ATOM 1862 CB LEU A 250 6.372 22.242 −5.781 1.00 13.57 C ATOM 1863 CG LEU A 250 6.739 21.000 −6.584 1.00 13.57 C ATOM 1864 CD1 LEU A 250 6.708 21.270 −8.069 1.00 13.57 C ATOM 1865 CD2 LEU A 250 8.106 20.523 −6.160 1.00 13.57 C ATOM 1866 N MET A 251 3.275 22.077 −5.427 1.00 11.06 N ATOM 1867 CA MET A 251 2.020 21.338 −5.523 1.00 11.06 C ATOM 1868 C MET A 251 1.023 22.083 −6.391 1.00 11.06 C ATOM 1869 O MET A 251 0.342 21.491 −7.220 1.00 11.06 O ATOM 1870 CB MET A 251 1.410 21.111 −4.143 1.00 11.06 C ATOM 1871 CG MET A 251 1.990 19.941 −3.406 1.00 11.06 C ATOM 1872 SD MET A 251 1.607 18.407 −4.235 1.00 11.06 S ATOM 1873 CE MET A 251 −0.146 18.289 −3.906 1.00 11.06 C ATOM 1874 N GLU A 252 0.951 23.393 −6.196 1.00 32.88 N ATOM 1875 CA GLU A 252 −0.025 24.226 −6.878 1.00 32.88 C ATOM 1876 C GLU A 252 0.278 24.491 −8.347 1.00 32.88 C ATOM 1877 O GLU A 252 −0.614 24.395 −9.184 1.00 32.88 O ATOM 1878 CB GLU A 252 −0.149 25.557 −6.156 1.00 32.88 C ATOM 1879 CG GLU A 252 −0.726 26.645 −7.012 1.00 32.88 C ATOM 1880 CD GLU A 252 −1.061 27.874 −6.203 1.00 32.88 C ATOM 1881 OE1 GLU A 252 −0.658 28.985 −6.618 1.00 32.88 O ATOM 1882 OE2 GLU A 252 −1.716 27.725 −5.142 1.00 32.88 O ATOM 1883 N LEU A 253 1.528 24.822 −8.660 1.00 14.78 N ATOM 1884 CA LEU A 253 1.872 25.320 −9.988 1.00 14.78 C ATOM 1885 C LEU A 253 2.270 24.243 −10.987 1.00 14.78 C ATOM 1886 O LEU A 253 2.397 24.514 −12.182 1.00 14.78 O ATOM 1887 CB LEU A 253 2.965 26.387 −9.901 1.00 14.78 C ATOM 1888 CG LEU A 253 2.656 27.659 −9.089 1.00 14.78 C ATOM 1889 CD1 LEU A 253 3.782 28.685 −9.193 1.00 14.78 C ATOM 1890 CD2 LEU A 253 1.328 28.301 −9.477 1.00 14.78 C ATOM 1891 N ALA A 254 2.462 23.020 −10.512 1.00 13.47 N ATOM 1892 CA ALA A 254 2.775 21.919 −11.414 1.00 13.47 C ATOM 1893 C ALA A 254 1.508 21.429 −12.087 1.00 13.47 C ATOM 1894 O ALA A 254 0.427 21.507 −11.513 1.00 13.47 O ATOM 1895 CB ALA A 254 3.426 20.790 −10.662 1.00 13.47 C ATOM 1896 N LYS A 255 1.634 20.910 −13.300 1.00 34.17 N ATOM 1897 CA LYS A 255 0.468 20.383 −14.002 1.00 34.17 C ATOM 1898 C LYS A 255 0.430 18.856 −13.974 1.00 34.17 C ATOM 1899 O LYS A 255 −0.267 18.219 −14.759 1.00 34.17 O ATOM 1900 CB LYS A 255 0.417 20.901 −15.438 1.00 34.17 C ATOM 1901 CG LYS A 255 0.330 22.415 −15.541 1.00 34.17 C ATOM 1902 CD LYS A 255 −0.588 22.977 −14.475 1.00 34.17 C ATOM 1903 CE LYS A 255 −1.081 24.371 −14.839 1.00 34.17 C ATOM 1904 NZ LYS A 255 0.004 25.220 −15.402 1.00 34.17 N ATOM 1905 N SER A 256 1.175 18.277 −13.047 1.00 4.00 N ATOM 1906 CA SER A 256 1.216 16.840 −12.891 1.00 4.00 C ATOM 1907 C SER A 256 −0.114 16.351 −12.387 1.00 4.00 C ATOM 1908 O SER A 256 −0.670 16.935 −11.464 1.00 4.00 O ATOM 1909 CB SER A 256 2.317 16.468 −11.912 1.00 4.00 C ATOM 1910 OG SER A 256 3.580 16.744 −12.483 1.00 4.00 O ATOM 1911 N GLN A 257 −0.616 15.281 −13.002 1.00 35.17 N ATOM 1912 CA GLN A 257 −1.895 14.685 −12.616 1.00 35.17 C ATOM 1913 C GLN A 257 −1.728 13.728 −11.425 1.00 35.17 C ATOM 1914 O GLN A 257 −2.707 13.300 −10.813 1.00 35.17 O ATOM 1915 CB GLN A 257 −2.550 13.963 −13.807 1.00 35.17 C ATOM 1916 CG GLN A 257 −2.708 14.804 −15.101 1.00 35.17 C ATOM 1917 CD GLN A 257 −4.012 15.611 −15.181 1.00 35.17 C ATOM 1918 OE1 GLN A 257 −5.072 15.146 −14.765 1.00 35.17 O ATOM 1919 NE2 GLN A 257 −3.931 16.817 −15.736 1.00 35.17 N ATOM 1920 N ASP A 258 −0.475 13.405 −11.103 1.00 7.80 N ATOM 1921 CA ASP A 258 −0.149 12.593 −9.932 1.00 7.80 C ATOM 1922 C ASP A 258 0.735 13.377 −8.976 1.00 7.80 C ATOM 1923 O ASP A 258 1.930 13.126 −8.885 1.00 7.80 O ATOM 1924 CB ASP A 258 0.561 11.296 −10.340 1.00 7.80 C ATOM 1925 CG ASP A 258 0.592 10.258 −9.215 1.00 7.80 C ATOM 1926 OD1 ASP A 258 0.355 10.625 −8.039 1.00 7.80 O ATOM 1927 OD2 ASP A 258 0.859 9.072 −9.517 1.00 7.80 O ATOM 1928 N LYS A 259 0.141 14.331 −8.272 1.00 16.34 N ATOM 1929 CA LYS A 259 0.844 15.070 −7.234 1.00 16.34 C ATOM 1930 C LYS A 259 0.546 14.451 −5.877 1.00 16.34 C ATOM 1931 O LYS A 259 −0.498 13.839 −5.682 1.00 16.34 O ATOM 1932 CB LYS A 259 0.408 16.535 −7.226 1.00 16.34 C ATOM 1933 CG LYS A 259 0.351 17.193 −8.594 1.00 16.34 C ATOM 1934 CD LYS A 259 0.225 18.696 −8.442 1.00 16.34 C ATOM 1935 CE LYS A 259 −0.490 19.326 −9.603 1.00 16.34 C ATOM 1936 NZ LYS A 259 −0.945 20.690 −9.252 1.00 16.34 N ATOM 1937 N THR A 260 1.462 14.619 −4.935 1.00 12.41 N ATOM 1938 CA THR A 260 1.258 14.128 −3.582 1.00 12.41 C ATOM 1939 C THR A 260 2.227 14.851 −2.660 1.00 12.41 C ATOM 1940 O THR A 260 3.438 14.749 −2.825 1.00 12.41 O ATOM 1941 CB THR A 260 1.498 12.609 −3.488 1.00 12.41 C ATOM 1942 OG1 THR A 260 1.060 11.965 −4.693 1.00 12.41 O ATOM 1943 CG2 THR A 260 0.755 12.027 −2.305 1.00 12.41 C ATOM 1944 N LEU A 261 1.696 15.597 −1.701 1.00 5.15 N ATOM 1945 CA LEU A 261 2.540 16.327 −0.771 1.00 5.15 C ATOM 1946 C LEU A 261 2.291 15.894 0.659 1.00 5.15 C ATOM 1947 O LEU A 261 1.144 15.849 1.116 1.00 5.15 O ATOM 1948 CB LEU A 261 2.289 17.831 −0.886 1.00 5.15 C ATOM 1949 CG LEU A 261 2.473 18.701 0.370 1.00 5.15 C ATOM 1950 CD1 LEU A 261 3.928 18.768 0.807 1.00 5.15 C ATOM 1951 CD2 LEU A 261 1.944 20.106 0.153 1.00 5.15 C ATOM 1952 N LYS A 262 3.370 15.596 1.377 1.00 6.23 N ATOM 1953 CA LYS A 262 3.266 15.321 2.805 1.00 6.23 C ATOM 1954 C LYS A 262 4.068 16.329 3.644 1.00 6.23 C ATOM 1955 O LYS A 262 5.178 16.699 3.286 1.00 6.23 O ATOM 1956 CB LYS A 262 3.681 13.876 3.115 1.00 6.23 C ATOM 1957 CG LYS A 262 3.562 13.544 4.577 1.00 6.23 C ATOM 1958 CD LYS A 262 3.389 12.072 4.848 1.00 6.23 C ATOM 1959 CE LYS A 262 3.149 11.866 6.341 1.00 6.23 C ATOM 1960 NZ LYS A 262 2.770 10.463 6.678 1.00 6.23 N ATOM 1961 N ILE A 263 3.486 16.792 4.743 1.00 7.83 N ATOM 1962 CA ILE A 263 4.202 17.628 5.692 1.00 7.83 C ATOM 1963 C ILE A 263 4.456 16.849 6.985 1.00 7.83 C ATOM 1964 O ILE A 263 3.599 16.076 7.449 1.00 7.83 O ATOM 1965 CB ILE A 263 3.427 18.935 5.994 1.00 7.83 C ATOM 1966 CG1 ILE A 263 3.199 19.739 4.711 1.00 7.83 C ATOM 1967 CG2 ILE A 263 4.153 19.789 7.037 1.00 7.83 C ATOM 1968 CD1 ILE A 263 4.474 20.295 4.082 1.00 7.83 C ATOM 1969 N TYR A 264 5.652 17.040 7.541 1.00 6.30 N ATOM 1970 CA TYR A 264 6.014 16.499 8.840 1.00 6.30 C ATOM 1971 C TYR A 264 6.197 17.644 9.818 1.00 6.30 C ATOM 1972 O TYR A 264 7.237 18.283 9.822 1.00 6.30 O ATOM 1973 CB TYR A 264 7.315 15.726 8.732 1.00 6.30 C ATOM 1974 CG TYR A 264 7.230 14.469 7.897 1.00 6.30 C ATOM 1975 CD1 TYR A 264 6.937 13.240 8.486 1.00 6.30 C ATOM 1976 CD2 TYR A 264 7.461 14.501 6.527 1.00 6.30 C ATOM 1977 CE1 TYR A 264 6.868 12.090 7.737 1.00 6.30 C ATOM 1978 CE2 TYR A 264 7.394 13.346 5.774 1.00 6.30 C ATOM 1979 CZ TYR A 264 7.096 12.148 6.391 1.00 6.30 C ATOM 1980 OH TYR A 264 7.030 10.997 5.664 1.00 6.30 O ATOM 1981 N GLU A 265 5.180 17.895 10.641 1.00 6.34 N ATOM 1982 CA GLU A 265 5.139 19.061 11.524 1.00 6.34 C ATOM 1983 C GLU A 265 6.240 19.095 12.577 1.00 6.34 C ATOM 1984 O GLU A 265 6.317 18.226 13.434 1.00 6.34 O ATOM 1985 CB GLU A 265 3.783 19.152 12.219 1.00 6.34 C ATOM 1986 CG GLU A 265 3.620 20.386 13.103 1.00 6.34 C ATOM 1987 CD GLU A 265 3.352 21.678 12.318 1.00 6.34 C ATOM 1988 OE1 GLU A 265 3.593 21.707 11.094 1.00 6.34 O ATOM 1989 OE2 GLU A 265 2.906 22.675 12.931 1.00 6.34 O ATOM 1990 N GLY A 266 7.074 20.123 12.514 1.00 8.50 N ATOM 1991 CA GLY A 266 8.154 20.288 13.461 1.00 8.50 C ATOM 1992 C GLY A 266 9.462 19.766 12.910 1.00 8.50 C ATOM 1993 O GLY A 266 10.536 20.132 13.382 1.00 8.50 O ATOM 1994 N ALA A 267 9.368 18.904 11.901 1.00 22.20 N ATOM 1995 CA ALA A 267 10.539 18.276 11.294 1.00 22.20 C ATOM 1996 C ALA A 267 11.487 19.305 10.666 1.00 22.20 C ATOM 1997 O ALA A 267 11.097 20.425 10.349 1.00 22.20 O ATOM 1998 CB ALA A 267 10.113 17.234 10.266 1.00 22.20 C ATOM 1999 N TYR A 268 12.739 18.907 10.492 1.00 8.04 N ATOM 2000 CA TYR A 268 13.750 19.802 9.976 1.00 8.04 C ATOM 2001 C TYR A 268 13.918 19.656 8.480 1.00 8.04 C ATOM 2002 O TYR A 268 12.947 19.539 7.750 1.00 8.04 O ATOM 2003 CB TYR A 268 15.062 19.536 10.683 1.00 8.04 C ATOM 2004 CG TYR A 268 15.162 20.226 12.021 1.00 8.04 C ATOM 2005 CD1 TYR A 268 14.043 20.399 12.823 1.00 8.04 C ATOM 2006 CD2 TYR A 268 16.380 20.699 12.485 1.00 8.04 C ATOM 2007 CE1 TYR A 268 14.139 21.032 14.041 1.00 8.04 C ATOM 2008 CE2 TYR A 268 16.480 21.329 13.694 1.00 8.04 C ATOM 2009 CZ TYR A 268 15.363 21.491 14.469 1.00 8.04 C ATOM 2010 OH TYR A 268 15.494 22.111 15.685 1.00 8.04 O ATOM 2011 N HIS A 269 15.155 19.661 8.018 1.00 9.34 N ATOM 2012 CA HIS A 269 15.394 19.611 6.581 1.00 9.34 C ATOM 2013 C HIS A 269 15.660 18.207 6.030 1.00 9.34 C ATOM 2014 O HIS A 269 14.904 17.685 5.212 1.00 9.34 O ATOM 2015 CB HIS A 269 16.550 20.536 6.214 1.00 9.34 C ATOM 2016 CG HIS A 269 16.820 20.604 4.745 1.00 9.34 C ATOM 2017 ND1 HIS A 269 15.955 21.209 3.857 1.00 9.34 N ATOM 2018 CD2 HIS A 269 17.859 20.147 4.008 1.00 9.34 C ATOM 2019 CE1 HIS A 269 16.451 21.123 2.636 1.00 9.34 C ATOM 2020 NE2 HIS A 269 17.609 20.488 2.701 1.00 9.34 N ATOM 2021 N VAL A 270 16.765 17.618 6.453 1.00 20.33 N ATOM 2022 CA VAL A 270 17.095 16.282 6.028 1.00 20.33 C ATOM 2023 C VAL A 270 16.102 15.371 6.710 1.00 20.33 C ATOM 2024 O VAL A 270 16.338 14.904 7.819 1.00 20.33 O ATOM 2025 CB VAL A 270 18.509 15.927 6.455 1.00 20.33 C ATOM 2026 CG1 VAL A 270 19.048 14.790 5.606 1.00 20.33 C ATOM 2027 CG2 VAL A 270 19.394 17.156 6.328 1.00 20.33 C ATOM 2028 N LEU A 271 14.971 15.147 6.056 1.00 15.05 N ATOM 2029 CA LEU A 271 13.902 14.343 6.638 1.00 15.05 C ATOM 2030 C LEU A 271 14.252 12.856 6.658 1.00 15.05 C ATOM 2031 O LEU A 271 13.711 12.093 7.454 1.00 15.05 O ATOM 2032 CB LEU A 271 12.594 14.543 5.867 1.00 15.05 C ATOM 2033 CG LEU A 271 12.160 15.969 5.523 1.00 15.05 C ATOM 2034 CD1 LEU A 271 10.843 15.972 4.778 1.00 15.05 C ATOM 2035 CD2 LEU A 271 12.040 16.779 6.783 1.00 15.05 C ATOM 2036 N HIS A 272 15.148 12.446 5.769 1.00 7.91 N ATOM 2037 CA HIS A 272 15.542 11.045 5.693 1.00 7.91 C ATOM 2038 C HIS A 272 16.608 10.725 6.725 1.00 7.91 C ATOM 2039 O HIS A 272 17.194 9.642 6.717 1.00 7.91 O ATOM 2040 CB HIS A 272 16.013 10.671 4.284 1.00 7.91 C ATOM 2041 CG HIS A 272 17.028 11.603 3.711 1.00 7.91 C ATOM 2042 ND1 HIS A 272 16.778 12.943 3.504 1.00 7.91 N ATOM 2043 CD2 HIS A 272 18.288 11.385 3.273 1.00 7.91 C ATOM 2044 CE1 HIS A 272 17.847 13.509 2.977 1.00 7.91 C ATOM 2045 NE2 HIS A 272 18.779 12.585 2.825 1.00 7.91 N ATOM 2046 N LYS A 273 16.845 11.679 7.615 1.00 7.13 N ATOM 2047 CA LYS A 273 17.787 11.497 8.700 1.00 7.13 C ATOM 2048 C LYS A 273 17.323 12.347 9.862 1.00 7.13 C ATOM 2049 O LYS A 273 18.113 13.073 10.467 1.00 7.13 O ATOM 2050 CB LYS A 273 19.206 11.905 8.280 1.00 7.13 C ATOM 2051 CG LYS A 273 19.605 11.434 6.896 1.00 7.13 C ATOM 2052 CD LYS A 273 21.104 11.313 6.750 1.00 7.13 C ATOM 2053 CE LYS A 273 21.452 10.581 5.466 1.00 7.13 C ATOM 2054 NZ LYS A 273 22.906 10.594 5.229 1.00 7.13 N ATOM 2055 N GLU A 274 16.033 12.265 10.164 1.00 10.28 N ATOM 2056 CA GLU A 274 15.462 12.983 11.301 1.00 10.28 C ATOM 2057 C GLU A 274 15.191 12.059 12.476 1.00 10.28 C ATOM 2058 O GLU A 274 15.676 10.927 12.519 1.00 10.28 O ATOM 2059 CB GLU A 274 14.161 13.663 10.898 1.00 10.28 C ATOM 2060 CG GLU A 274 14.268 15.169 10.753 1.00 10.28 C ATOM 2061 CD GLU A 274 14.020 15.890 12.060 1.00 10.28 C ATOM 2062 OE1 GLU A 274 14.414 17.070 12.160 1.00 10.28 O ATOM 2063 OE2 GLU A 274 13.435 15.273 12.979 1.00 10.28 O ATOM 2064 N LEU A 275 14.408 12.537 13.431 1.00 10.03 N ATOM 2065 CA LEU A 275 13.987 11.666 14.503 1.00 10.03 C ATOM 2066 C LEU A 275 13.483 10.396 13.827 1.00 10.03 C ATOM 2067 O LEU A 275 13.027 10.449 12.681 1.00 10.03 O ATOM 2068 CB LEU A 275 12.894 12.339 15.323 1.00 10.03 C ATOM 2069 CG LEU A 275 13.263 13.695 15.928 1.00 10.03 C ATOM 2070 CD1 LEU A 275 12.175 14.170 16.869 1.00 10.03 C ATOM 2071 CD2 LEU A 275 14.578 13.611 16.656 1.00 10.03 C ATOM 2072 N PRO A 276 13.572 9.244 14.516 1.00 15.64 N ATOM 2073 CA PRO A 276 13.249 7.957 13.889 1.00 15.64 C ATOM 2074 C PRO A 276 11.832 7.891 13.329 1.00 15.64 C ATOM 2075 O PRO A 276 11.660 7.577 12.151 1.00 15.64 O ATOM 2076 CB PRO A 276 13.395 6.962 15.040 1.00 15.64 C ATOM 2077 CG PRO A 276 14.250 7.634 16.027 1.00 15.64 C ATOM 2078 CD PRO A 276 13.910 9.083 15.938 1.00 15.64 C ATOM 2079 N GLU A 277 10.834 8.181 14.156 1.00 25.18 N ATOM 2080 CA GLU A 277 9.448 8.093 13.715 1.00 25.18 C ATOM 2081 C GLU A 277 9.251 8.802 12.380 1.00 25.18 C ATOM 2082 O GLU A 277 8.477 8.365 11.530 1.00 25.18 O ATOM 2083 CB GLU A 277 8.496 8.667 14.766 1.00 25.18 C ATOM 2084 CG GLU A 277 8.628 10.176 14.979 1.00 25.18 C ATOM 2085 CD GLU A 277 9.321 10.532 16.292 1.00 25.18 C ATOM 2086 OE1 GLU A 277 8.795 11.400 17.025 1.00 25.18 O ATOM 2087 OE2 GLU A 277 10.383 9.939 16.594 1.00 25.18 O ATOM 2088 N VAL A 278 9.970 9.899 12.201 1.00 9.49 N ATOM 2089 CA VAL A 278 9.869 10.675 10.980 1.00 9.49 C ATOM 2090 C VAL A 278 10.535 9.941 9.847 1.00 9.49 C ATOM 2091 O VAL A 278 9.869 9.490 8.925 1.00 9.49 O ATOM 2092 CB VAL A 278 10.531 12.041 11.120 1.00 9.49 C ATOM 2093 CG1 VAL A 278 10.743 12.648 9.757 1.00 9.49 C ATOM 2094 CG2 VAL A 278 9.688 12.950 12.008 1.00 9.49 C ATOM 2095 N THR A 279 11.855 9.816 9.917 1.00 4.63 N ATOM 2096 CA THR A 279 12.597 9.166 8.845 1.00 4.63 C ATOM 2097 C THR A 279 11.853 7.931 8.375 1.00 4.63 C ATOM 2098 O THR A 279 11.703 7.705 7.182 1.00 4.63 O ATOM 2099 CB THR A 279 14.015 8.783 9.283 1.00 4.63 C ATOM 2100 OG1 THR A 279 14.658 9.928 9.857 1.00 4.63 O ATOM 2101 CG2 THR A 279 14.829 8.304 8.098 1.00 4.63 C ATOM 2102 N ASN A 280 11.369 7.146 9.329 1.00 18.19 N ATOM 2103 CA ASN A 280 10.653 5.924 9.015 1.00 18.19 C ATOM 2104 C ASN A 280 9.435 6.209 8.170 1.00 18.19 C ATOM 2105 O ASN A 280 9.216 5.581 7.144 1.00 18.19 O ATOM 2106 CB ASN A 280 10.263 5.201 10.297 1.00 18.19 C ATOM 2107 CG ASN A 280 11.447 4.524 10.957 1.00 18.19 C ATOM 2108 OD1 ASN A 280 12.435 4.198 10.295 1.00 18.19 O ATOM 2109 ND2 ASN A 280 11.354 4.302 12.261 1.00 18.19 N ATOM 2110 N SER A 281 8.636 7.168 8.607 1.00 34.10 N ATOM 2111 CA SER A 281 7.517 7.619 7.806 1.00 34.10 C ATOM 2112 C SER A 281 8.019 7.882 6.401 1.00 34.10 C ATOM 2113 O SER A 281 7.404 7.483 5.417 1.00 34.10 O ATOM 2114 CB SER A 281 6.948 8.902 8.390 1.00 34.10 C ATOM 2115 OG SER A 281 6.132 9.559 7.446 1.00 34.10 O ATOM 2116 N VAL A 282 9.159 8.551 6.323 1.00 25.09 N ATOM 2117 CA VAL A 282 9.745 8.926 5.050 1.00 25.09 C ATOM 2118 C VAL A 282 10.117 7.700 4.217 1.00 25.09 C ATOM 2119 O VAL A 282 9.770 7.618 3.039 1.00 25.09 O ATOM 2120 CB VAL A 282 10.973 9.821 5.261 1.00 25.09 C ATOM 2121 CG1 VAL A 282 11.621 10.123 3.951 1.00 25.09 C ATOM 2122 CG2 VAL A 282 10.569 11.107 5.938 1.00 25.09 C ATOM 2123 N PHE A 283 10.812 6.744 4.832 1.00 4.11 N ATOM 2124 CA PHE A 283 11.191 5.500 4.153 1.00 4.11 C ATOM 2125 C PHE A 283 9.967 4.743 3.678 1.00 4.11 C ATOM 2126 O PHE A 283 9.941 4.216 2.569 1.00 4.11 O ATOM 2127 CB PHE A 283 12.047 4.617 5.067 1.00 4.11 C ATOM 2128 CG PHE A 283 13.505 4.946 5.019 1.00 4.11 C ATOM 2129 CD1 PHE A 283 13.951 6.222 5.329 1.00 4.11 C ATOM 2130 CD2 PHE A 283 14.433 3.996 4.641 1.00 4.11 C ATOM 2131 CE1 PHE A 283 15.306 6.549 5.262 1.00 4.11 C ATOM 2132 CE2 PHE A 283 15.787 4.312 4.578 1.00 4.11 C ATOM 2133 CZ PHE A 283 16.220 5.594 4.888 1.00 4.11 C ATOM 2134 N HIS A 284 8.947 4.718 4.523 1.00 11.48 N ATOM 2135 CA HIS A 284 7.724 4.003 4.221 1.00 11.48 C ATOM 2136 C HIS A 284 7.006 4.589 3.024 1.00 11.48 C ATOM 2137 O HIS A 284 6.728 3.890 2.053 1.00 11.48 O ATOM 2138 CB HIS A 284 6.794 4.049 5.422 1.00 11.48 C ATOM 2139 CG HIS A 284 5.560 3.227 5.253 1.00 11.48 C ATOM 2140 ND1 HIS A 284 5.532 1.870 5.498 1.00 11.48 N ATOM 2141 CD2 HIS A 284 4.312 3.566 4.856 1.00 11.48 C ATOM 2142 CE1 HIS A 284 4.316 1.411 5.268 1.00 11.48 C ATOM 2143 NE2 HIS A 284 3.557 2.419 4.875 1.00 11.48 N ATOM 2144 N GLU A 285 6.704 5.878 3.110 1.00 10.06 N ATOM 2145 CA GLU A 285 5.938 6.570 2.079 1.00 10.06 C ATOM 2146 C GLU A 285 6.579 6.413 0.706 1.00 10.06 C ATOM 2147 O GLU A 285 5.891 6.148 −0.287 1.00 10.06 O ATOM 2148 CB GLU A 285 5.795 8.055 2.423 1.00 10.06 C ATOM 2149 CG GLU A 285 5.320 8.324 3.835 1.00 10.06 C ATOM 2150 CD GLU A 285 3.915 7.835 4.078 1.00 10.06 C ATOM 2151 OE1 GLU A 285 3.138 7.755 3.102 1.00 10.06 O ATOM 2152 OE2 GLU A 285 3.587 7.528 5.246 1.00 10.06 O ATOM 2153 N ILE A 286 7.895 6.588 0.659 1.00 16.72 N ATOM 2154 CA ILE A 286 8.624 6.434 −0.585 1.00 16.72 C ATOM 2155 C ILE A 286 8.526 4.998 −1.050 1.00 16.72 C ATOM 2156 O ILE A 286 8.326 4.728 −2.239 1.00 16.72 O ATOM 2157 CB ILE A 286 10.105 6.765 −0.426 1.00 16.72 C ATOM 2158 CG1 ILE A 286 10.298 8.086 0.315 1.00 16.72 C ATOM 2159 CG2 ILE A 286 10.765 6.813 −1.784 1.00 16.72 C ATOM 2160 CD1 ILE A 286 11.719 8.276 0.831 1.00 16.72 C ATOM 2161 N ASN A 287 8.681 4.070 −0.113 1.00 5.01 N ATOM 2162 CA ASN A 287 8.560 2.668 −0.464 1.00 5.01 C ATOM 2163 C ASN A 287 7.311 2.464 −1.316 1.00 5.01 C ATOM 2164 O ASN A 287 7.365 1.922 −2.418 1.00 5.01 O ATOM 2165 CB ASN A 287 8.505 1.792 0.788 1.00 5.01 C ATOM 2166 CG ASN A 287 8.476 0.310 0.462 1.00 5.01 C ATOM 2167 OD1 ASN A 287 7.497 −0.187 −0.076 1.00 5.01 O ATOM 2168 ND2 ASN A 287 9.546 −0.404 0.802 1.00 5.01 N ATOM 2169 N MET A 288 6.183 2.943 −0.822 1.00 8.24 N ATOM 2170 CA MET A 288 4.929 2.655 −1.480 1.00 8.24 C ATOM 2171 C MET A 288 4.688 3.487 −2.708 1.00 8.24 C ATOM 2172 O MET A 288 4.256 2.950 −3.715 1.00 8.24 O ATOM 2173 CB MET A 288 3.797 2.767 −0.491 1.00 8.24 C ATOM 2174 CG MET A 288 4.133 1.957 0.726 1.00 8.24 C ATOM 2175 SD MET A 288 2.772 0.980 1.328 1.00 8.24 S ATOM 2176 CE MET A 288 1.848 2.304 2.152 1.00 8.24 C ATOM 2177 N TRP A 289 4.970 4.785 −2.642 1.00 21.83 N ATOM 2178 CA TRP A 289 4.807 5.640 −3.811 1.00 21.83 C ATOM 2179 C TRP A 289 5.424 4.937 −5.000 1.00 21.83 C ATOM 2180 O TRP A 289 4.799 4.806 −6.045 1.00 21.83 O ATOM 2181 CB TRP A 289 5.475 6.994 −3.602 1.00 21.83 C ATOM 2182 CG TRP A 289 5.014 8.045 −4.584 1.00 21.83 C ATOM 2183 CD1 TRP A 289 3.895 8.819 −4.487 1.00 21.83 C ATOM 2184 CD2 TRP A 289 5.661 8.434 −5.805 1.00 21.83 C ATOM 2185 NE1 TRP A 289 3.803 9.663 −5.567 1.00 21.83 N ATOM 2186 CE2 TRP A 289 4.875 9.444 −6.390 1.00 21.83 C ATOM 2187 CE3 TRP A 289 6.826 8.027 −6.456 1.00 21.83 C ATOM 2188 CZ2 TRP A 289 5.219 10.051 −7.592 1.00 21.83 C ATOM 2189 CZ3 TRP A 289 7.163 8.632 −7.644 1.00 21.83 C ATOM 2190 CH2 TRP A 289 6.365 9.632 −8.201 1.00 21.83 C ATOM 2191 N VAL A 290 6.647 4.457 −4.816 1.00 4.10 N ATOM 2192 CA VAL A 290 7.357 3.730 −5.861 1.00 4.10 C ATOM 2193 C VAL A 290 6.743 2.383 −6.176 1.00 4.10 C ATOM 2194 O VAL A 290 6.366 2.121 −7.309 1.00 4.10 O ATOM 2195 CB VAL A 290 8.799 3.470 −5.463 1.00 4.10 C ATOM 2196 CG1 VAL A 290 9.484 2.649 −6.541 1.00 4.10 C ATOM 2197 CG2 VAL A 290 9.524 4.793 −5.209 1.00 4.10 C ATOM 2198 N SER A 291 6.667 1.530 −5.161 1.00 11.26 N ATOM 2199 CA SER A 291 6.120 0.184 −5.295 1.00 11.26 C ATOM 2200 C SER A 291 4.841 0.142 −6.107 1.00 11.26 C ATOM 2201 O SER A 291 4.678 −0.714 −6.985 1.00 11.26 O ATOM 2202 CB SER A 291 5.849 −0.400 −3.917 1.00 11.26 C ATOM 2203 OG SER A 291 7.035 −0.396 −3.159 1.00 11.26 O ATOM 2204 N GLN A 292 3.939 1.064 −5.791 1.00 57.84 N ATOM 2205 CA GLN A 292 2.634 1.138 −6.427 1.00 57.84 C ATOM 2206 C GLN A 292 2.750 1.619 −7.859 1.00 57.84 C ATOM 2207 O GLN A 292 1.955 1.246 −8.710 1.00 57.84 O ATOM 2208 CB GLN A 292 1.710 2.059 −5.632 1.00 57.84 C ATOM 2209 CG GLN A 292 1.616 1.701 −4.151 1.00 57.84 C ATOM 2210 CD GLN A 292 1.042 0.302 −3.904 1.00 57.84 C ATOM 2211 OE1 GLN A 292 0.133 −0.144 −4.610 1.00 57.84 O ATOM 2212 NE2 GLN A 292 1.565 −0.387 −2.890 1.00 57.84 N ATOM 2213 N ARG A 293 3.739 2.458 −8.127 1.00 13.45 N ATOM 2214 CA ARG A 293 4.047 2.804 −9.504 1.00 13.45 C ATOM 2215 C ARG A 293 5.024 1.776 −10.038 1.00 13.45 C ATOM 2216 O ARG A 293 5.909 2.076 −10.833 1.00 13.45 O ATOM 2217 CB ARG A 293 4.594 4.216 −9.596 1.00 13.45 C ATOM 2218 CG ARG A 293 3.515 5.230 −9.395 1.00 13.45 C ATOM 2219 CD ARG A 293 4.019 6.425 −8.646 1.00 13.45 C ATOM 2220 NE ARG A 293 2.929 7.330 −8.290 1.00 13.45 N ATOM 2221 CZ ARG A 293 2.171 7.203 −7.208 1.00 13.45 C ATOM 2222 NH1 ARG A 293 2.380 6.205 −6.354 1.00 13.45 N ATOM 2223 NH2 ARG A 293 1.201 8.076 −6.980 1.00 13.45 N ATOM 2224 N THR A 294 4.821 0.542 −9.591 1.00 15.51 N ATOM 2225 CA THR A 294 5.747 −0.544 −9.858 1.00 15.51 C ATOM 2226 C THR A 294 5.088 −1.900 −9.619 1.00 15.51 C ATOM 2227 O THR A 294 4.921 −2.685 −10.550 1.00 15.51 O ATOM 2228 CB THR A 294 6.997 −0.409 −8.971 1.00 15.51 C ATOM 2229 OG1 THR A 294 8.068 0.179 −9.723 1.00 15.51 O ATOM 2230 CG2 THR A 294 7.415 −1.761 −8.432 1.00 15.51 C ATOM 2231 N ARG B 9 45.389 35.996 −23.066 1.00 50.60 N ATOM 2232 CA ARG B 9 44.424 35.585 −22.050 1.00 50.60 C ATOM 2233 C ARG B 9 43.259 36.569 −21.933 1.00 50.60 C ATOM 2234 O ARG B 9 43.378 37.748 −22.279 1.00 50.60 O ATOM 2235 CB ARG B 9 45.101 35.480 −20.688 1.00 50.60 C ATOM 2236 CG ARG B 9 46.523 34.981 −20.740 1.00 50.60 C ATOM 2237 CD ARG B 9 47.353 35.615 −19.642 1.00 50.60 C ATOM 2238 NE ARG B 9 48.387 34.708 −19.162 1.00 50.60 N ATOM 2239 CZ ARG B 9 48.289 33.981 −18.052 1.00 50.60 C ATOM 2240 NH1 ARG B 9 47.206 34.064 −17.286 1.00 50.60 N ATOM 2241 NH2 ARG B 9 49.282 33.173 −17.704 1.00 50.60 N ATOM 2242 N THR B 10 42.131 36.083 −21.426 1.00 59.93 N ATOM 2243 CA THR B 10 40.984 36.945 −21.186 1.00 59.93 C ATOM 2244 C THR B 10 41.400 38.086 −20.276 1.00 59.93 C ATOM 2245 O THR B 10 42.450 38.023 −19.633 1.00 59.93 O ATOM 2246 CB THR B 10 39.840 36.188 −20.496 1.00 59.93 C ATOM 2247 OG1 THR B 10 40.138 36.046 −19.103 1.00 59.93 O ATOM 2248 CG2 THR B 10 39.652 34.818 −21.121 1.00 59.93 C ATOM 2249 N PRO B 11 40.583 39.144 −20.228 1.00 58.60 N ATOM 2250 CA PRO B 11 40.816 40.175 −19.221 1.00 58.60 C ATOM 2251 C PRO B 11 40.885 39.524 −17.848 1.00 58.60 C ATOM 2252 O PRO B 11 41.716 39.913 −17.026 1.00 58.60 O ATOM 2253 CB PRO B 11 39.568 41.049 −19.326 1.00 58.60 C ATOM 2254 CG PRO B 11 39.108 40.873 −20.721 1.00 58.60 C ATOM 2255 CD PRO B 11 39.437 39.460 −21.096 1.00 58.60 C ATOM 2256 N GLN B 12 40.028 38.531 −17.616 1.00 46.49 N ATOM 2257 CA GLN B 12 39.981 37.837 −16.331 1.00 46.49 C ATOM 2258 C GLN B 12 41.074 36.783 −16.196 1.00 46.49 C ATOM 2259 O GLN B 12 41.050 35.965 −15.281 1.00 46.49 O ATOM 2260 CB GLN B 12 38.608 37.214 −16.096 1.00 46.49 C ATOM 2261 CG GLN B 12 37.533 38.227 −15.730 1.00 46.49 C ATOM 2262 CD GLN B 12 36.869 38.848 −16.946 1.00 46.49 C ATOM 2263 OE1 GLN B 12 37.206 38.524 −18.084 1.00 46.49 O ATOM 2264 NE2 GLN B 12 35.912 39.739 −16.709 1.00 46.49 N ATOM 2265 N SER B 13 42.018 36.803 −17.129 1.00 38.64 N ATOM 2266 CA SER B 13 43.274 36.076 −16.974 1.00 38.64 C ATOM 2267 C SER B 13 43.221 34.616 −17.418 1.00 38.64 C ATOM 2268 O SER B 13 44.033 33.802 −16.982 1.00 38.64 O ATOM 2269 CB SER B 13 43.779 36.175 −15.529 1.00 38.64 C ATOM 2270 OG SER B 13 43.813 37.520 −15.087 1.00 38.64 O ATOM 2271 N ILE B 14 42.280 34.290 −18.295 1.00 33.69 N ATOM 2272 CA ILE B 14 42.198 32.940 −18.830 1.00 33.69 C ATOM 2273 C ILE B 14 42.844 32.863 −20.217 1.00 33.69 C ATOM 2274 O ILE B 14 42.389 33.515 −21.156 1.00 33.69 O ATOM 2275 CB ILE B 14 40.739 32.440 −18.910 1.00 33.69 C ATOM 2276 CG1 ILE B 14 39.992 32.754 −17.615 1.00 33.69 C ATOM 2277 CG2 ILE B 14 40.703 30.948 −19.191 1.00 33.69 C ATOM 2278 CD1 ILE B 14 40.562 32.071 −16.406 1.00 33.69 C ATOM 2279 N PRO B 15 43.915 32.061 −20.342 1.00 29.98 N ATOM 2280 CA PRO B 15 44.575 31.860 −21.634 1.00 29.98 C ATOM 2281 C PRO B 15 43.572 31.585 −22.752 1.00 29.98 C ATOM 2282 O PRO B 15 42.919 30.538 −22.771 1.00 29.98 O ATOM 2283 CB PRO B 15 45.447 30.630 −21.384 1.00 29.98 C ATOM 2284 CG PRO B 15 45.787 30.720 −19.929 1.00 29.98 C ATOM 2285 CD PRO B 15 44.568 31.299 −19.260 1.00 29.98 C ATOM 2286 N TYR B 16 43.458 32.536 −23.675 1.00 48.84 N ATOM 2287 CA TYR B 16 42.537 32.409 −24.795 1.00 48.84 C ATOM 2288 C TYR B 16 42.786 31.129 −25.569 1.00 48.84 C ATOM 2289 O TYR B 16 41.861 30.561 −26.142 1.00 48.84 O ATOM 2290 CB TYR B 16 42.669 33.593 −25.754 1.00 48.84 C ATOM 2291 CG TYR B 16 41.901 34.830 −25.353 1.00 48.84 C ATOM 2292 CD1 TYR B 16 40.513 34.826 −25.302 1.00 48.84 C ATOM 2293 CD2 TYR B 16 42.565 36.007 −25.048 1.00 48.84 C ATOM 2294 CE1 TYR B 16 39.814 35.955 −24.944 1.00 48.84 C ATOM 2295 CE2 TYR B 16 41.875 37.145 −24.689 1.00 48.84 C ATOM 2296 CZ TYR B 16 40.501 37.118 −24.637 1.00 48.84 C ATOM 2297 OH TYR B 16 39.814 38.262 −24.274 1.00 48.84 O ATOM 2298 N GLN B 17 44.041 30.690 −25.598 1.00 59.62 N ATOM 2299 CA GLN B 17 44.425 29.489 −26.332 1.00 59.62 C ATOM 2300 C GLN B 17 43.491 28.316 −26.029 1.00 59.62 C ATOM 2301 O GLN B 17 43.369 27.388 −26.826 1.00 59.62 O ATOM 2302 CB GLN B 17 45.872 29.091 −26.002 1.00 59.62 C ATOM 2303 CG GLN B 17 46.895 30.238 −25.987 1.00 59.62 C ATOM 2304 CD GLN B 17 48.350 29.747 −25.924 1.00 59.62 C ATOM 2305 OE1 GLN B 17 48.902 29.255 −26.913 1.00 59.62 O ATOM 2306 NE2 GLN B 17 48.975 29.898 −24.761 1.00 59.62 N ATOM 2307 N ASP B 18 42.827 28.370 −24.878 1.00 77.53 N ATOM 2308 CA ASP B 18 42.005 27.261 −24.405 1.00 77.53 C ATOM 2309 C ASP B 18 40.507 27.550 −24.519 1.00 77.53 C ATOM 2310 O ASP B 18 39.679 26.677 −24.257 1.00 77.53 O ATOM 2311 CB ASP B 18 42.359 26.941 −22.951 1.00 77.53 C ATOM 2312 CG ASP B 18 43.836 27.148 −22.650 1.00 77.53 C ATOM 2313 OD1 ASP B 18 44.680 26.590 −23.384 1.00 77.53 O ATOM 2314 OD2 ASP B 18 44.149 27.868 −21.676 1.00 77.53 O ATOM 2315 N LEU B 19 40.168 28.780 −24.897 1.00 72.50 N ATOM 2316 CA LEU B 19 38.771 29.197 −25.037 1.00 72.50 C ATOM 2317 C LEU B 19 38.366 29.332 −26.510 1.00 72.50 C ATOM 2318 O LEU B 19 39.231 29.416 −27.387 1.00 72.50 O ATOM 2319 CB LEU B 19 38.537 30.521 −24.305 1.00 72.50 C ATOM 2320 CG LEU B 19 38.847 30.545 −22.810 1.00 72.50 C ATOM 2321 CD1 LEU B 19 38.403 31.863 −22.194 1.00 72.50 C ATOM 2322 CD2 LEU B 19 38.181 29.367 −22.113 1.00 72.50 C ATOM 2323 N PRO B 20 37.047 29.339 −26.786 1.00 41.11 N ATOM 2324 CA PRO B 20 36.553 29.517 −28.156 1.00 41.11 C ATOM 2325 C PRO B 20 36.705 30.973 −28.539 1.00 41.11 C ATOM 2326 O PRO B 20 36.478 31.843 −27.693 1.00 41.11 O ATOM 2327 CB PRO B 20 35.063 29.168 −28.048 1.00 41.11 C ATOM 2328 CG PRO B 20 34.875 28.578 −26.688 1.00 41.11 C ATOM 2329 CD PRO B 20 35.945 29.155 −25.832 1.00 41.11 C ATOM 2330 N HIS B 21 37.077 31.251 −29.781 1.00 50.34 N ATOM 2331 CA HIS B 21 37.344 32.630 −30.142 1.00 50.34 C ATOM 2332 C HIS B 21 37.569 32.858 −31.625 1.00 50.34 C ATOM 2333 O HIS B 21 37.451 31.949 −32.446 1.00 50.34 O ATOM 2334 CB HIS B 21 38.581 33.114 −29.384 1.00 50.34 C ATOM 2335 CG HIS B 21 39.785 32.243 −29.581 1.00 50.34 C ATOM 2336 ND1 HIS B 21 40.663 31.942 −28.561 1.00 50.34 N ATOM 2337 CD2 HIS B 21 40.252 31.600 −30.679 1.00 50.34 C ATOM 2338 CE1 HIS B 21 41.622 31.159 −29.024 1.00 50.34 C ATOM 2339 NE2 HIS B 21 41.395 30.935 −30.306 1.00 50.34 N ATOM 2340 N LEU B 22 37.869 34.111 −31.940 1.00 36.34 N ATOM 2341 CA LEU B 22 38.515 34.502 −33.185 1.00 36.34 C ATOM 2342 C LEU B 22 38.930 35.951 −33.019 1.00 36.34 C ATOM 2343 O LEU B 22 38.638 36.559 −31.987 1.00 36.34 O ATOM 2344 CB LEU B 22 37.624 34.311 −34.419 1.00 36.34 C ATOM 2345 CG LEU B 22 36.149 34.717 −34.413 1.00 36.34 C ATOM 2346 CD1 LEU B 22 35.865 35.898 −33.481 1.00 36.34 C ATOM 2347 CD2 LEU B 22 35.707 35.014 −35.845 1.00 36.34 C ATOM 2348 N VAL B 23 39.597 36.506 −34.027 1.00 9.29 N ATOM 2349 CA VAL B 23 40.194 37.828 −33.875 1.00 9.29 C ATOM 2350 C VAL B 23 39.517 38.967 −34.632 1.00 9.29 C ATOM 2351 O VAL B 23 39.576 39.068 −35.853 1.00 9.29 O ATOM 2352 CB VAL B 23 41.714 37.817 −34.140 1.00 9.29 C ATOM 2353 CG1 VAL B 23 42.272 39.217 −34.072 1.00 9.29 C ATOM 2354 CG2 VAL B 23 42.406 36.946 −33.110 1.00 9.29 C ATOM 2355 N ASN B 24 38.856 39.805 −33.849 1.00 36.38 N ATOM 2356 CA ASN B 24 38.458 41.137 −34.249 1.00 36.38 C ATOM 2357 C ASN B 24 39.324 41.652 −35.393 1.00 36.38 C ATOM 2358 O ASN B 24 40.538 41.478 −35.381 1.00 36.38 O ATOM 2359 CB ASN B 24 38.608 42.041 −33.023 1.00 36.38 C ATOM 2360 CG ASN B 24 38.028 43.425 −33.225 1.00 36.38 C ATOM 2361 OD1 ASN B 24 38.524 44.204 −34.031 1.00 36.38 O ATOM 2362 ND2 ASN B 24 36.988 43.749 −32.461 1.00 36.38 N ATOM 2363 N ALA B 25 38.704 42.287 −36.383 1.00 46.50 N ATOM 2364 CA ALA B 25 39.454 42.856 −37.497 1.00 46.50 C ATOM 2365 C ALA B 25 40.465 43.871 −36.976 1.00 46.50 C ATOM 2366 O ALA B 25 41.350 44.319 −37.709 1.00 46.50 O ATOM 2367 CB ALA B 25 38.517 43.499 −38.503 1.00 46.50 C ATOM 2368 N ASP B 26 40.326 44.221 −35.700 1.00 46.73 N ATOM 2369 CA ASP B 26 41.214 45.174 −35.053 1.00 46.73 C ATOM 2370 C ASP B 26 42.145 44.488 −34.069 1.00 46.73 C ATOM 2371 O ASP B 26 42.616 45.114 −33.114 1.00 46.73 O ATOM 2372 CB ASP B 26 40.406 46.255 −34.345 1.00 46.73 C ATOM 2373 CG ASP B 26 39.640 47.122 −35.315 1.00 46.73 C ATOM 2374 OD1 ASP B 26 40.051 47.184 −36.491 1.00 46.73 O ATOM 2375 OD2 ASP B 26 38.635 47.745 −34.912 1.00 46.73 O ATOM 2376 N GLY B 27 42.409 43.205 −34.315 1.00 35.00 N ATOM 2377 CA GLY B 27 43.344 42.434 −33.513 1.00 35.00 C ATOM 2378 C GLY B 27 42.915 42.247 −32.071 1.00 35.00 C ATOM 2379 O GLY B 27 43.727 42.386 −31.151 1.00 35.00 O ATOM 2380 N GLN B 28 41.637 41.935 −31.872 1.00 36.74 N ATOM 2381 CA GLN B 28 41.105 41.720 −30.533 1.00 36.74 C ATOM 2382 C GLN B 28 40.476 40.350 −30.390 1.00 36.74 C ATOM 2383 O GLN B 28 39.627 39.955 −31.190 1.00 36.74 O ATOM 2384 CB GLN B 28 40.076 42.781 −30.186 1.00 36.74 C ATOM 2385 CG GLN B 28 40.670 44.076 −29.730 1.00 36.74 C ATOM 2386 CD GLN B 28 39.715 45.236 −29.941 1.00 36.74 C ATOM 2387 OE1 GLN B 28 38.690 45.093 −30.615 1.00 36.74 O ATOM 2388 NE2 GLN B 28 40.048 46.398 −29.375 1.00 36.74 N ATOM 2389 N TYR B 29 40.903 39.629 −29.360 1.00 59.63 N ATOM 2390 CA TYR B 29 40.371 38.306 −29.085 1.00 59.63 C ATOM 2391 C TYR B 29 38.933 38.407 −28.580 1.00 59.63 C ATOM 2392 O TYR B 29 38.648 39.157 −27.643 1.00 59.63 O ATOM 2393 CB TYR B 29 41.268 37.565 −28.082 1.00 59.63 C ATOM 2394 CG TYR B 29 42.443 36.846 −28.722 1.00 59.63 C ATOM 2395 CD1 TYR B 29 43.685 37.463 −28.851 1.00 59.63 C ATOM 2396 CD2 TYR B 29 42.303 35.547 −29.199 1.00 59.63 C ATOM 2397 CE1 TYR B 29 44.752 36.803 −29.441 1.00 59.63 C ATOM 2398 CE2 TYR B 29 43.358 34.881 −29.788 1.00 59.63 C ATOM 2399 CZ TYR B 29 44.579 35.508 −29.909 1.00 59.63 C ATOM 2400 OH TYR B 29 45.620 34.821 −30.498 1.00 59.63 O ATOM 2401 N LEU B 30 38.030 37.666 −29.219 1.00 49.98 N ATOM 2402 CA LEU B 30 36.634 37.625 −28.791 1.00 49.98 C ATOM 2403 C LEU B 30 36.281 36.242 −28.265 1.00 49.98 C ATOM 2404 O LEU B 30 36.536 35.235 −28.931 1.00 49.98 O ATOM 2405 CB LEU B 30 35.700 38.005 −29.940 1.00 49.98 C ATOM 2406 CG LEU B 30 35.885 39.418 −30.494 1.00 49.98 C ATOM 2407 CD1 LEU B 30 35.357 39.486 −31.914 1.00 49.98 C ATOM 2408 CD2 LEU B 30 35.228 40.475 −29.606 1.00 49.98 C ATOM 2409 N PHE B 31 35.707 36.198 −27.064 1.00 7.41 N ATOM 2410 CA PHE B 31 35.322 34.928 −26.448 1.00 7.41 C ATOM 2411 C PHE B 31 34.035 34.396 −27.056 1.00 7.41 C ATOM 2412 O PHE B 31 33.018 35.100 −27.087 1.00 7.41 O ATOM 2413 CB PHE B 31 35.143 35.086 −24.938 1.00 7.41 C ATOM 2414 CG PHE B 31 34.508 33.900 −24.286 1.00 7.41 C ATOM 2415 CD1 PHE B 31 35.248 32.766 −24.023 1.00 7.41 C ATOM 2416 CD2 PHE B 31 33.169 33.913 −23.942 1.00 7.41 C ATOM 2417 CE1 PHE B 31 34.669 31.664 −23.417 1.00 7.41 C ATOM 2418 CE2 PHE B 31 32.582 32.814 −23.341 1.00 7.41 C ATOM 2419 CZ PHE B 31 33.332 31.687 −23.078 1.00 7.41 C ATOM 2420 N CYS B 32 34.083 33.154 −27.533 1.00 25.28 N ATOM 2421 CA CYS B 32 32.931 32.542 −28.189 1.00 25.28 C ATOM 2422 C CYS B 32 32.221 31.485 −27.352 1.00 25.28 C ATOM 2423 O CYS B 32 32.775 30.922 −26.402 1.00 25.28 O ATOM 2424 CB CYS B 32 33.325 31.933 −29.527 1.00 25.28 C ATOM 2425 SG CYS B 32 33.914 33.127 −30.688 1.00 25.28 S ATOM 2426 N ARG B 33 30.986 31.204 −27.747 1.00 29.48 N ATOM 2427 CA ARG B 33 30.128 30.310 −27.005 1.00 29.48 C ATOM 2428 C ARG B 33 29.245 29.604 −28.020 1.00 29.48 C ATOM 2429 O ARG B 33 28.762 30.239 −28.960 1.00 29.48 O ATOM 2430 CB ARG B 33 29.290 31.138 −26.038 1.00 29.48 C ATOM 2431 CG ARG B 33 28.808 30.415 −24.807 1.00 29.48 C ATOM 2432 CD ARG B 33 28.099 31.392 −23.893 1.00 29.48 C ATOM 2433 NE ARG B 33 29.020 32.086 −23.008 1.00 29.48 N ATOM 2434 CZ ARG B 33 29.121 31.824 −21.713 1.00 29.48 C ATOM 2435 NH1 ARG B 33 28.348 30.893 −21.181 1.00 29.48 N ATOM 2436 NH2 ARG B 33 29.978 32.491 −20.953 1.00 29.48 N ATOM 2437 N TYR B 34 29.054 28.295 −27.848 1.00 31.99 N ATOM 2438 CA TYR B 34 28.261 27.498 −28.787 1.00 31.99 C ATOM 2439 C TYR B 34 27.412 26.439 −28.090 1.00 31.99 C ATOM 2440 O TYR B 34 27.849 25.849 −27.106 1.00 31.99 O ATOM 2441 CB TYR B 34 29.178 26.803 −29.788 1.00 31.99 C ATOM 2442 CG TYR B 34 30.195 27.713 −30.427 1.00 31.99 C ATOM 2443 CD1 TYR B 34 29.993 28.222 −31.703 1.00 31.99 C ATOM 2444 CD2 TYR B 34 31.363 28.065 −29.758 1.00 31.99 C ATOM 2445 CE1 TYR B 34 30.922 29.057 −32.295 1.00 31.99 C ATOM 2446 CE2 TYR B 34 32.299 28.896 −30.343 1.00 31.99 C ATOM 2447 CZ TYR B 34 32.072 29.388 −31.610 1.00 31.99 C ATOM 2448 OH TYR B 34 32.995 30.217 −32.196 1.00 31.99 O ATOM 2449 N TRP B 35 26.204 26.204 −28.604 1.00 13.49 N ATOM 2450 CA TRP B 35 25.340 25.118 −28.127 1.00 13.49 C ATOM 2451 C TRP B 35 24.815 24.364 −29.330 1.00 13.49 C ATOM 2452 O TRP B 35 23.969 24.880 −30.050 1.00 13.49 O ATOM 2453 CB TRP B 35 24.126 25.648 −27.358 1.00 13.49 C ATOM 2454 CG TRP B 35 24.420 26.654 −26.286 1.00 13.49 C ATOM 2455 CD1 TRP B 35 24.296 26.479 −24.934 1.00 13.49 C ATOM 2456 CD2 TRP B 35 24.868 27.995 −26.476 1.00 13.49 C ATOM 2457 NE1 TRP B 35 24.643 27.629 −24.276 1.00 13.49 N ATOM 2458 CE2 TRP B 35 24.998 28.576 −25.202 1.00 13.49 C ATOM 2459 CE3 TRP B 35 25.177 28.761 −27.600 1.00 13.49 C ATOM 2460 CZ2 TRP B 35 25.422 29.879 −25.025 1.00 13.49 C ATOM 2461 CZ3 TRP B 35 25.599 30.048 −27.421 1.00 13.49 C ATOM 2462 CH2 TRP B 35 25.719 30.597 −26.146 1.00 13.49 C ATOM 2463 N ALA B 36 25.296 23.147 −29.551 1.00 29.40 N ATOM 2464 CA ALA B 36 24.922 22.413 −30.755 1.00 29.40 C ATOM 2465 C ALA B 36 24.333 21.045 −30.440 1.00 29.40 C ATOM 2466 CB ALA B 36 26.115 22.282 −31.695 1.00 29.40 C ATOM 2467 O ALA B 36 24.804 20.347 −29.540 1.00 29.40 O ATOM 2468 N PRO B 37 23.290 20.663 −31.189 1.00 48.43 N ATOM 2469 CA PRO B 37 22.572 19.395 −31.012 1.00 48.43 C ATOM 2470 C PRO B 37 23.439 18.226 −31.451 1.00 48.43 C ATOM 2471 O PRO B 37 24.441 18.436 −32.141 1.00 48.43 O ATOM 2472 CB PRO B 37 21.393 19.537 −31.976 1.00 48.43 C ATOM 2473 CG PRO B 37 21.896 20.497 −33.025 1.00 48.43 C ATOM 2474 CD PRO B 37 22.668 21.499 −32.231 1.00 48.43 C ATOM 2475 N THR B 38 23.056 17.015 −31.060 1.00 47.93 N ATOM 2476 CA THR B 38 23.787 15.821 −31.456 1.00 47.93 C ATOM 2477 C THR B 38 23.571 15.528 −32.933 1.00 47.93 C ATOM 2478 O THR B 38 24.501 15.140 −33.642 1.00 47.93 O ATOM 2479 CB THR B 38 23.345 14.598 −30.646 1.00 47.93 C ATOM 2480 OG1 THR B 38 21.953 14.345 −30.880 1.00 47.93 O ATOM 2481 CG2 THR B 38 23.577 14.829 −29.163 1.00 47.93 C ATOM 2482 N GLY B 39 22.339 15.730 −33.390 1.00 64.78 N ATOM 2483 CA GLY B 39 21.972 15.453 −34.768 1.00 64.78 C ATOM 2484 C GLY B 39 22.510 16.461 −35.766 1.00 64.78 C ATOM 2485 O GLY B 39 23.563 17.062 −35.554 1.00 64.78 O ATOM 2486 N THR B 40 21.783 16.642 −36.864 1.00 61.16 N ATOM 2487 CA THR B 40 22.193 17.577 −37.905 1.00 61.16 C ATOM 2488 C THR B 40 21.502 18.926 −37.744 1.00 61.16 C ATOM 2489 O THR B 40 20.276 19.015 −37.836 1.00 61.16 O ATOM 2490 CB THR B 40 21.877 17.038 −39.317 1.00 61.16 C ATOM 2491 OG1 THR B 40 22.489 15.753 −39.505 1.00 61.16 O ATOM 2492 CG2 THR B 40 22.378 18.016 −40.384 1.00 61.16 C ATOM 2493 N PRO B 41 22.294 19.984 −37.511 1.00 50.06 N ATOM 2494 CA PRO B 41 21.780 21.347 −37.317 1.00 50.06 C ATOM 2495 C PRO B 41 20.731 21.736 −38.357 1.00 50.06 C ATOM 2496 O PRO B 41 21.066 21.836 −39.535 1.00 50.06 O ATOM 2497 CB PRO B 41 23.031 22.212 −37.495 1.00 50.06 C ATOM 2498 CG PRO B 41 24.161 21.328 −37.063 1.00 50.06 C ATOM 2499 CD PRO B 41 23.767 19.925 −37.442 1.00 50.06 C ATOM 2500 N LYS B 42 19.486 21.943 −37.928 1.00 43.15 N ATOM 2501 CA LYS B 42 18.446 22.453 −38.818 1.00 43.15 C ATOM 2502 C LYS B 42 18.843 23.831 −39.328 1.00 43.15 C ATOM 2503 O LYS B 42 18.730 24.125 −40.518 1.00 43.15 O ATOM 2504 CB LYS B 42 17.107 22.574 −38.093 1.00 43.15 C ATOM 2505 CG LYS B 42 16.232 21.334 −38.083 1.00 43.15 C ATOM 2506 CD LYS B 42 14.775 21.746 −37.865 1.00 43.15 C ATOM 2507 CE LYS B 42 13.906 20.605 −37.374 1.00 43.15 C ATOM 2508 NZ LYS B 42 12.461 20.924 −37.524 1.00 43.15 N ATOM 2509 N ALA B 43 19.290 24.687 −38.417 1.00 52.83 N ATOM 2510 CA ALA B 43 19.786 25.998 −38.808 1.00 52.83 C ATOM 2511 C ALA B 43 20.703 26.574 −37.743 1.00 52.83 C ATOM 2512 O ALA B 43 21.008 25.916 −36.746 1.00 52.83 O ATOM 2513 CB ALA B 43 18.634 26.949 −39.093 1.00 52.83 C ATOM 2514 N LEU B 44 21.135 27.808 −37.966 1.00 38.86 N ATOM 2515 CA LEU B 44 22.036 28.489 −37.055 1.00 38.86 C ATOM 2516 C LEU B 44 21.356 29.727 −36.479 1.00 38.86 C ATOM 2517 O LEU B 44 20.409 30.245 −37.072 1.00 38.86 O ATOM 2518 CB LEU B 44 23.300 28.896 −37.812 1.00 38.86 C ATOM 2519 CG LEU B 44 23.991 27.777 −38.606 1.00 38.86 C ATOM 2520 CD1 LEU B 44 24.763 28.312 −39.809 1.00 38.86 C ATOM 2521 CD2 LEU B 44 24.903 26.973 −37.699 1.00 38.86 C ATOM 2522 N ILE B 45 21.830 30.197 −35.326 1.00 12.46 N ATOM 2523 CA ILE B 45 21.324 31.443 −34.742 1.00 12.46 C ATOM 2524 C ILE B 45 22.311 32.115 −33.785 1.00 12.46 C ATOM 2525 O ILE B 45 22.800 31.512 −32.826 1.00 12.46 O ATOM 2526 CB ILE B 45 19.985 31.238 −34.035 1.00 12.46 C ATOM 2527 CG1 ILE B 45 19.507 32.552 −33.422 1.00 12.46 C ATOM 2528 CG2 ILE B 45 20.105 30.118 −33.003 1.00 12.46 C ATOM 2529 CD1 ILE B 45 18.094 32.508 −32.935 1.00 12.46 C ATOM 2530 N PHE B 46 22.591 33.383 −34.066 1.00 28.28 N ATOM 2531 CA PHE B 46 23.575 34.134 −33.313 1.00 28.28 C ATOM 2532 C PHE B 46 22.912 35.000 −32.271 1.00 28.28 C ATOM 2533 O PHE B 46 21.927 35.667 −32.550 1.00 28.28 O ATOM 2534 CB PHE B 46 24.393 35.011 −34.241 1.00 28.28 C ATOM 2535 CG PHE B 46 25.429 35.806 −33.535 1.00 28.28 C ATOM 2536 CD1 PHE B 46 25.115 37.037 −32.980 1.00 28.28 C ATOM 2537 CD2 PHE B 46 26.716 35.321 −33.411 1.00 28.28 C ATOM 2538 CE1 PHE B 46 26.068 37.782 −32.322 1.00 28.28 C ATOM 2539 CE2 PHE B 46 27.680 36.051 −32.755 1.00 28.28 C ATOM 2540 CZ PHE B 46 27.357 37.291 −32.208 1.00 28.28 C ATOM 2541 N VAL B 47 23.479 35.007 −31.073 1.00 7.01 N ATOM 2542 CA VAL B 47 22.845 35.638 −29.924 1.00 7.01 C ATOM 2543 C VAL B 47 23.574 36.897 −29.493 1.00 7.01 C ATOM 2544 O VAL B 47 24.733 36.850 −29.104 1.00 7.01 O ATOM 2545 CB VAL B 47 22.764 34.649 −28.728 1.00 7.01 C ATOM 2546 CG1 VAL B 47 22.222 35.344 −27.474 1.00 7.01 C ATOM 2547 CG2 VAL B 47 21.918 33.439 −29.107 1.00 7.01 C ATOM 2548 N SER B 48 22.887 38.025 −29.550 1.00 4.75 N ATOM 2549 CA SER B 48 23.531 39.296 −29.252 1.00 4.75 C ATOM 2550 C SER B 48 23.173 39.843 −27.864 1.00 4.75 C ATOM 2551 O SER B 48 22.092 40.411 −27.660 1.00 4.75 O ATOM 2552 CB SER B 48 23.215 40.328 −30.343 1.00 4.75 C ATOM 2553 OG SER B 48 23.920 41.532 −30.123 1.00 4.75 O ATOM 2554 N HIS B 49 24.091 39.674 −26.915 1.00 20.39 N ATOM 2555 CA HIS B 49 23.921 40.235 −25.581 1.00 20.39 C ATOM 2556 C HIS B 49 23.948 41.759 −25.628 1.00 20.39 C ATOM 2557 O HIS B 49 24.484 42.355 −26.561 1.00 20.39 O ATOM 2558 CB HIS B 49 24.970 39.683 −24.601 1.00 20.39 C ATOM 2559 CG HIS B 49 26.348 40.255 −24.770 1.00 20.39 C ATOM 2560 ND1 HIS B 49 26.646 41.577 −24.511 1.00 20.39 N ATOM 2561 CD2 HIS B 49 27.516 39.670 −25.127 1.00 20.39 C ATOM 2562 CE1 HIS B 49 27.933 41.787 −24.723 1.00 20.39 C ATOM 2563 NE2 HIS B 49 28.484 40.646 −25.099 1.00 20.39 N ATOM 2564 N GLY B 50 23.358 42.388 −24.622 1.00 21.66 N ATOM 2565 CA GLY B 50 23.231 43.829 −24.608 1.00 21.66 C ATOM 2566 C GLY B 50 24.407 44.520 −23.958 1.00 21.66 C ATOM 2567 O GLY B 50 25.437 43.904 −23.682 1.00 21.66 O ATOM 2568 N ALA B 51 24.243 45.816 −23.720 1.00 42.07 N ATOM 2569 CA ALA B 51 25.262 46.611 −23.055 1.00 42.07 C ATOM 2570 C ALA B 51 25.450 46.103 −21.636 1.00 42.07 C ATOM 2571 O ALA B 51 24.570 45.460 −21.076 1.00 42.07 O ATOM 2572 CB ALA B 51 24.874 48.086 −23.052 1.00 42.07 C ATOM 2573 N GLY B 52 26.611 46.372 −21.061 1.00 23.99 N ATOM 2574 CA GLY B 52 26.869 45.994 −19.691 1.00 23.99 C ATOM 2575 C GLY B 52 27.066 44.509 −19.509 1.00 23.99 C ATOM 2576 O GLY B 52 27.919 44.094 −18.736 1.00 23.99 O ATOM 2577 N GLU B 53 26.293 43.704 −20.226 1.00 23.65 N ATOM 2578 CA GLU B 53 26.257 42.266 −19.962 1.00 23.65 C ATOM 2579 C GLU B 53 27.148 41.439 −20.880 1.00 23.65 C ATOM 2580 O GLU B 53 28.170 41.914 −21.367 1.00 23.65 O ATOM 2581 CB GLU B 53 24.816 41.744 −20.000 1.00 23.65 C ATOM 2582 CG GLU B 53 24.027 42.169 −21.217 1.00 23.65 C ATOM 2583 CD GLU B 53 22.786 41.340 −21.419 1.00 23.65 C ATOM 2584 OE1 GLU B 53 22.478 40.483 −20.565 1.00 23.65 O ATOM 2585 OE2 GLU B 53 22.117 41.548 −22.445 1.00 23.65 O ATOM 2586 N HIS B 54 26.765 40.193 −21.108 1.00 15.04 N ATOM 2587 CA HIS B 54 27.587 39.320 −21.923 1.00 15.04 C ATOM 2588 C HIS B 54 26.807 38.112 −22.387 1.00 15.04 C ATOM 2589 O HIS B 54 25.602 38.012 −22.139 1.00 15.04 O ATOM 2590 CB HIS B 54 28.807 38.864 −21.132 1.00 15.04 C ATOM 2591 CG HIS B 54 28.461 38.181 −19.847 1.00 15.04 C ATOM 2592 ND1 HIS B 54 28.607 36.824 −19.663 1.00 15.04 N ATOM 2593 CD2 HIS B 54 27.948 38.666 −18.691 1.00 15.04 C ATOM 2594 CE1 HIS B 54 28.206 36.504 −18.446 1.00 15.04 C ATOM 2595 NE2 HIS B 54 27.803 37.603 −17.837 1.00 15.04 N ATOM 2596 N SER B 55 27.509 37.193 −23.048 1.00 5.43 N ATOM 2597 CA SER B 55 26.887 36.000 −23.617 1.00 5.43 C ATOM 2598 C SER B 55 26.489 34.974 −22.565 1.00 5.43 C ATOM 2599 O SER B 55 25.626 34.130 −22.808 1.00 5.43 O ATOM 2600 CB SER B 55 27.799 35.348 −24.669 1.00 5.43 C ATOM 2601 OG SER B 55 28.925 34.706 −24.088 1.00 5.43 O ATOM 2602 N GLY B 56 27.119 35.047 −21.399 1.00 25.67 N ATOM 2603 CA GLY B 56 26.844 34.096 −20.345 1.00 25.67 C ATOM 2604 C GLY B 56 25.367 33.976 −20.030 1.00 25.67 C ATOM 2605 O GLY B 56 24.882 32.881 −19.721 1.00 25.67 O ATOM 2606 N ARG B 57 24.655 35.101 −20.136 1.00 6.99 N ATOM 2607 CA ARG B 57 23.283 35.239 −19.630 1.00 6.99 C ATOM 2608 C ARG B 57 22.173 34.683 −20.540 1.00 6.99 C ATOM 2609 O ARG B 57 21.002 34.624 −20.157 1.00 6.99 O ATOM 2610 CB ARG B 57 23.005 36.704 −19.332 1.00 6.99 C ATOM 2611 CG ARG B 57 24.142 37.393 −18.613 1.00 6.99 C ATOM 2612 CD ARG B 57 23.942 38.908 −18.515 1.00 6.99 C ATOM 2613 NE ARG B 57 22.634 39.273 −17.986 1.00 6.99 N ATOM 2614 CZ ARG B 57 22.240 39.044 −16.737 1.00 6.99 C ATOM 2615 NH1 ARG B 57 23.059 38.447 −15.886 1.00 6.99 N ATOM 2616 NH2 ARG B 57 21.029 39.414 −16.338 1.00 6.99 N ATOM 2617 N TYR B 58 22.539 34.268 −21.743 1.00 10.85 N ATOM 2618 CA TYR B 58 21.556 33.727 −22.663 1.00 10.85 C ATOM 2619 C TYR B 58 21.635 32.211 −22.720 1.00 10.85 C ATOM 2620 O TYR B 58 21.334 31.610 −23.748 1.00 10.85 O ATOM 2621 CB TYR B 58 21.761 34.335 −24.043 1.00 10.85 C ATOM 2622 CG TYR B 58 21.533 35.825 −24.039 1.00 10.85 C ATOM 2623 CD1 TYR B 58 22.502 36.696 −23.558 1.00 10.85 C ATOM 2624 CD2 TYR B 58 20.346 36.359 −24.492 1.00 10.85 C ATOM 2625 CE1 TYR B 58 22.292 38.057 −23.539 1.00 10.85 C ATOM 2626 CE2 TYR B 58 20.131 37.708 −24.477 1.00 10.85 C ATOM 2627 CZ TYR B 58 21.101 38.557 −24.000 1.00 10.85 C ATOM 2628 OH TYR B 58 20.862 39.912 −23.994 1.00 10.85 O ATOM 2629 N GLU B 59 22.031 31.603 −21.606 1.00 48.25 N ATOM 2630 CA GLU B 59 22.237 30.163 −21.547 1.00 48.25 C ATOM 2631 C GLU B 59 20.923 29.408 −21.664 1.00 48.25 C ATOM 2632 O GLU B 59 20.801 28.471 −22.447 1.00 48.25 O ATOM 2633 CB GLU B 59 22.936 29.780 −20.244 1.00 48.25 C ATOM 2634 CG GLU B 59 23.436 28.345 −20.218 1.00 48.25 C ATOM 2635 CD GLU B 59 24.703 28.148 −21.041 1.00 48.25 C ATOM 2636 OE1 GLU B 59 25.440 29.140 −21.246 1.00 48.25 O ATOM 2637 OE2 GLU B 59 24.960 27.004 −21.482 1.00 48.25 O ATOM 2638 N GLU B 60 19.945 29.830 −20.873 1.00 16.51 N ATOM 2639 CA GLU B 60 18.617 29.230 −20.857 1.00 16.51 C ATOM 2640 C GLU B 60 17.922 29.299 −22.222 1.00 16.51 C ATOM 2641 O GLU B 60 17.275 28.353 −22.655 1.00 16.51 O ATOM 2642 CB GLU B 60 17.754 29.938 −19.809 1.00 16.51 C ATOM 2643 CG GLU B 60 18.556 30.644 −18.693 1.00 16.51 C ATOM 2644 CD GLU B 60 19.228 31.977 −19.127 1.00 16.51 C ATOM 2645 OE1 GLU B 60 20.162 32.433 −18.422 1.00 16.51 O ATOM 2646 OE2 GLU B 60 18.830 32.563 −20.162 1.00 16.51 O ATOM 2647 N LEU B 61 18.056 30.432 −22.895 1.00 8.98 N ATOM 2648 CA LEU B 61 17.414 30.638 −24.183 1.00 8.98 C ATOM 2649 C LEU B 61 18.039 29.775 −25.248 1.00 8.98 C ATOM 2650 O LEU B 61 17.343 29.199 −26.070 1.00 8.98 O ATOM 2651 CB LEU B 61 17.513 32.100 −24.601 1.00 8.98 C ATOM 2652 CG LEU B 61 16.616 33.054 −23.810 1.00 8.98 C ATOM 2653 CD1 LEU B 61 17.330 33.610 −22.586 1.00 8.98 C ATOM 2654 CD2 LEU B 61 16.145 34.174 −24.692 1.00 8.98 C ATOM 2655 N ALA B 62 19.361 29.699 −25.240 1.00 12.98 N ATOM 2656 CA ALA B 62 20.086 28.883 −26.195 1.00 12.98 C ATOM 2657 C ALA B 62 19.725 27.408 −26.046 1.00 12.98 C ATOM 2658 O ALA B 62 19.480 26.713 −27.032 1.00 12.98 O ATOM 2659 CB ALA B 62 21.565 29.077 −26.009 1.00 12.98 C ATOM 2660 N ARG B 63 19.701 26.926 −24.812 1.00 40.61 N ATOM 2661 CA ARG B 63 19.402 25.528 −24.567 1.00 40.61 C ATOM 2662 C ARG B 63 18.066 25.124 −25.145 1.00 40.61 C ATOM 2663 O ARG B 63 17.798 23.944 −25.358 1.00 40.61 O ATOM 2664 CB ARG B 63 19.436 25.243 −23.078 1.00 40.61 C ATOM 2665 CG ARG B 63 20.810 24.862 −22.615 1.00 40.61 C ATOM 2666 CD ARG B 63 21.107 25.398 −21.242 1.00 40.61 C ATOM 2667 NE ARG B 63 22.435 24.978 −20.823 1.00 40.61 N ATOM 2668 CZ ARG B 63 22.951 25.225 −19.629 1.00 40.61 C ATOM 2669 NH1 ARG B 63 22.242 25.902 −18.736 1.00 40.61 N ATOM 2670 NH2 ARG B 63 24.171 24.790 −19.332 1.00 40.61 N ATOM 2671 N MET B 64 17.218 26.104 −25.407 1.00 8.99 N ATOM 2672 CA MET B 64 15.926 25.804 −25.998 1.00 8.99 C ATOM 2673 C MET B 64 15.972 25.900 −27.515 1.00 8.99 C ATOM 2674 O MET B 64 15.280 25.174 −28.224 1.00 8.99 O ATOM 2675 CB MET B 64 14.845 26.727 −25.441 1.00 8.99 C ATOM 2676 CG MET B 64 13.615 26.801 −26.316 1.00 8.99 C ATOM 2677 SD MET B 64 13.472 28.366 −27.159 1.00 8.99 S ATOM 2678 CE MET B 64 13.132 29.380 −25.740 1.00 8.99 C ATOM 2679 N LEU B 65 16.788 26.803 −28.019 1.00 7.01 N ATOM 2680 CA LEU B 65 16.913 26.922 −29.450 1.00 7.01 C ATOM 2681 C LEU B 65 17.681 25.694 −29.872 1.00 7.01 C ATOM 2682 O LEU B 65 17.277 24.984 −30.785 1.00 7.01 O ATOM 2683 CB LEU B 65 17.642 28.221 −29.823 1.00 7.01 C ATOM 2684 CG LEU B 65 16.975 29.481 −29.241 1.00 7.01 C ATOM 2685 CD1 LEU B 65 17.931 30.648 −29.163 1.00 7.01 C ATOM 2686 CD2 LEU B 65 15.724 29.857 −30.023 1.00 7.01 C ATOM 2687 N MET B 66 18.775 25.427 −29.171 1.00 46.81 N ATOM 2688 CA MET B 66 19.601 24.267 −29.462 1.00 46.81 C ATOM 2689 C MET B 66 18.785 22.981 −29.330 1.00 46.81 C ATOM 2690 O MET B 66 18.916 22.066 −30.138 1.00 46.81 O ATOM 2691 CB MET B 66 20.843 24.259 −28.558 1.00 46.81 C ATOM 2692 CG MET B 66 21.753 23.054 −28.728 1.00 46.81 C ATOM 2693 SD MET B 66 21.340 21.756 −27.549 1.00 46.81 S ATOM 2694 CE MET B 66 21.700 22.628 −26.017 1.00 46.81 C ATOM 2695 N GLY B 67 17.935 22.925 −28.311 1.00 29.97 N ATOM 2696 CA GLY B 67 16.985 21.841 −28.173 1.00 29.97 C ATOM 2697 C GLY B 67 16.130 21.757 −29.419 1.00 29.97 C ATOM 2698 O GLY B 67 15.808 20.668 −29.869 1.00 29.97 O ATOM 2699 N LEU B 68 15.775 22.912 −29.981 1.00 14.22 N ATOM 2700 CA LEU B 68 14.998 22.976 −31.223 1.00 14.22 C ATOM 2701 C LEU B 68 15.838 22.500 −32.404 1.00 14.22 C ATOM 2702 O LEU B 68 15.458 22.649 −33.563 1.00 14.22 O ATOM 2703 CB LEU B 68 14.496 24.403 −31.493 1.00 14.22 C ATOM 2704 CG LEU B 68 13.245 24.967 −30.808 1.00 14.22 C ATOM 2705 CD1 LEU B 68 12.636 26.031 −31.680 1.00 14.22 C ATOM 2706 CD2 LEU B 68 12.225 23.893 −30.578 1.00 14.22 C ATOM 2707 N ASP B 69 16.991 21.929 −32.087 1.00 18.66 N ATOM 2708 CA ASP B 69 17.885 21.358 −33.088 1.00 18.66 C ATOM 2709 C ASP B 69 18.471 22.462 −33.949 1.00 18.66 C ATOM 2710 O ASP B 69 18.608 22.321 −35.163 1.00 18.66 O ATOM 2711 CB ASP B 69 17.189 20.264 −33.922 1.00 18.66 C ATOM 2712 CG ASP B 69 16.876 19.003 −33.096 1.00 18.66 C ATOM 2713 OD1 ASP B 69 15.731 18.503 −33.167 1.00 18.66 O ATOM 2714 OD2 ASP B 69 17.767 18.526 −32.357 1.00 18.66 O ATOM 2715 N LEU B 70 18.816 23.565 −33.295 1.00 16.63 N ATOM 2716 CA LEU B 70 19.562 24.640 −33.940 1.00 16.63 C ATOM 2717 C LEU B 70 20.940 24.733 −33.316 1.00 16.63 C ATOM 2718 O LEU B 70 21.116 24.430 −32.137 1.00 16.63 O ATOM 2719 CB LEU B 70 18.859 25.987 −33.781 1.00 16.63 C ATOM 2720 CG LEU B 70 17.833 26.405 −34.828 1.00 16.63 C ATOM 2721 CD1 LEU B 70 16.616 25.502 −34.795 1.00 16.63 C ATOM 2722 CD2 LEU B 70 17.440 27.840 −34.582 1.00 16.63 C ATOM 2723 N LEU B 71 21.921 25.140 −34.111 1.00 15.33 N ATOM 2724 CA LEU B 71 23.256 25.366 −33.591 1.00 15.33 C ATOM 2725 C LEU B 71 23.304 26.791 −33.106 1.00 15.33 C ATOM 2726 O LEU B 71 23.510 27.715 −33.895 1.00 15.33 O ATOM 2727 CB LEU B 71 24.310 25.176 −34.674 1.00 15.33 C ATOM 2728 CG LEU B 71 25.769 25.091 −34.208 1.00 15.33 C ATOM 2729 CD1 LEU B 71 26.706 25.406 −35.361 1.00 15.33 C ATOM 2730 CD2 LEU B 71 26.072 26.014 −33.044 1.00 15.33 C ATOM 2731 N VAL B 72 23.115 26.973 −31.809 1.00 10.44 N ATOM 2732 CA VAL B 72 23.227 28.304 −31.253 1.00 10.44 C ATOM 2733 C VAL B 72 24.699 28.668 −31.065 1.00 10.44 C ATOM 2734 O VAL B 72 25.493 27.883 −30.543 1.00 10.44 O ATOM 2735 CB VAL B 72 22.439 28.452 −29.946 1.00 10.44 C ATOM 2736 CG1 VAL B 72 22.596 29.857 −29.395 1.00 10.44 C ATOM 2737 CG2 VAL B 72 20.969 28.136 −30.192 1.00 10.44 C ATOM 2738 N PHE B 73 25.062 29.855 −31.536 1.00 31.44 N ATOM 2739 CA PHE B 73 26.405 30.357 −31.321 1.00 31.44 C ATOM 2740 C PHE B 73 26.394 31.839 −30.988 1.00 31.44 C ATOM 2741 O PHE B 73 25.407 32.536 −31.223 1.00 31.44 O ATOM 2742 CB PHE B 73 27.312 30.058 −32.515 1.00 31.44 C ATOM 2743 CG PHE B 73 26.968 30.825 −33.755 1.00 31.44 C ATOM 2744 CD1 PHE B 73 25.784 30.591 −34.425 1.00 31.44 C ATOM 2745 CD2 PHE B 73 27.850 31.767 −34.266 1.00 31.44 C ATOM 2746 CE1 PHE B 73 25.479 31.295 −35.573 1.00 31.44 C ATOM 2747 CE2 PHE B 73 27.552 32.474 −35.414 1.00 31.44 C ATOM 2748 CZ PHE B 73 26.366 32.240 −36.067 1.00 31.44 C ATOM 2749 N ALA B 74 27.503 32.307 −30.432 1.00 22.43 N ATOM 2750 CA ALA B 74 27.562 33.647 −29.895 1.00 22.43 C ATOM 2751 C ALA B 74 28.965 33.979 −29.382 1.00 22.43 C ATOM 2752 O ALA B 74 29.709 33.093 −28.951 1.00 22.43 O ATOM 2753 CB ALA B 74 26.544 33.776 −28.768 1.00 22.43 C ATOM 2754 N HIS B 75 29.315 35.263 −29.428 1.00 12.17 N ATOM 2755 CA HIS B 75 30.526 35.743 −28.780 1.00 12.17 C ATOM 2756 C HIS B 75 30.287 36.967 −27.883 1.00 12.17 C ATOM 2757 O HIS B 75 29.141 37.343 −27.602 1.00 12.17 O ATOM 2758 CB HIS B 75 31.599 36.044 −29.817 1.00 12.17 C ATOM 2759 CG HIS B 75 31.202 37.086 −30.811 1.00 12.17 C ATOM 2760 ND1 HIS B 75 30.867 36.783 −32.113 1.00 12.17 N ATOM 2761 CD2 HIS B 75 31.091 38.429 −30.694 1.00 12.17 C ATOM 2762 CE1 HIS B 75 30.567 37.894 −32.757 1.00 12.17 C ATOM 2763 NE2 HIS B 75 30.694 38.909 −31.918 1.00 12.17 N ATOM 2764 N ASP B 76 31.381 37.581 −27.437 1.00 34.86 N ATOM 2765 CA ASP B 76 31.310 38.714 −26.517 1.00 34.86 C ATOM 2766 C ASP B 76 31.821 40.027 −27.081 1.00 34.86 C ATOM 2767 O ASP B 76 33.027 40.239 −27.196 1.00 34.86 O ATOM 2768 CB ASP B 76 32.055 38.402 −25.225 1.00 34.86 C ATOM 2769 CG ASP B 76 31.138 37.904 −24.151 1.00 34.86 C ATOM 2770 OD1 ASP B 76 29.993 37.538 −24.483 1.00 34.86 O ATOM 2771 OD2 ASP B 76 31.555 37.891 −22.979 1.00 34.86 O ATOM 2772 N HIS B 77 30.883 40.913 −27.393 1.00 37.35 N ATOM 2773 CA HIS B 77 31.193 42.260 −27.866 1.00 37.35 C ATOM 2774 C HIS B 77 32.460 42.847 −27.244 1.00 37.35 C ATOM 2775 O HIS B 77 32.671 42.759 −26.036 1.00 37.35 O ATOM 2776 CB HIS B 77 30.008 43.185 −27.606 1.00 37.35 C ATOM 2777 CG HIS B 77 28.723 42.677 −28.174 1.00 37.35 C ATOM 2778 ND1 HIS B 77 28.586 42.326 −29.499 1.00 37.35 N ATOM 2779 CD2 HIS B 77 27.518 42.456 −27.599 1.00 37.35 C ATOM 2780 CE1 HIS B 77 27.350 41.914 −29.716 1.00 37.35 C ATOM 2781 NE2 HIS B 77 26.682 41.982 −28.579 1.00 37.35 N ATOM 2782 N VAL B 78 33.303 43.439 −28.084 1.00 50.16 N ATOM 2783 CA VAL B 78 34.547 44.050 −27.626 1.00 50.16 C ATOM 2784 C VAL B 78 34.292 44.980 −26.448 1.00 50.16 C ATOM 2785 CB VAL B 78 35.237 44.845 −28.763 1.00 50.16 C ATOM 2786 CG1 VAL B 78 34.423 46.082 −29.128 1.00 50.16 C ATOM 2787 CG2 VAL B 78 36.649 45.234 −28.359 1.00 50.16 C ATOM 2788 O VAL B 78 33.358 45.776 −26.469 1.00 50.16 O ATOM 2789 N GLY B 79 35.121 44.881 −25.418 1.00 58.12 N ATOM 2790 CA GLY B 79 34.913 45.677 −24.225 1.00 58.12 C ATOM 2791 C GLY B 79 33.814 45.072 −23.373 1.00 58.12 C ATOM 2792 O GLY B 79 33.233 45.741 −22.513 1.00 58.12 O ATOM 2793 N HIS B 80 33.530 43.795 −23.626 1.00 16.20 N ATOM 2794 CA HIS B 80 32.519 43.053 −22.873 1.00 16.20 C ATOM 2795 C HIS B 80 32.978 41.654 −22.498 1.00 16.20 C ATOM 2796 O HIS B 80 33.751 41.024 −23.222 1.00 16.20 O ATOM 2797 CB HIS B 80 31.213 42.945 −23.664 1.00 16.20 C ATOM 2798 CG HIS B 80 30.405 44.201 −23.657 1.00 16.20 C ATOM 2799 ND1 HIS B 80 30.615 45.219 −24.556 1.00 16.20 N ATOM 2800 CD2 HIS B 80 29.401 44.611 −22.850 1.00 16.20 C ATOM 2801 CE1 HIS B 80 29.767 46.200 −24.311 1.00 16.20 C ATOM 2802 NE2 HIS B 80 29.019 45.855 −23.282 1.00 16.20 N ATOM 2803 N GLY B 81 32.482 41.170 −21.365 1.00 34.83 N ATOM 2804 CA GLY B 81 32.747 39.814 −20.927 1.00 34.83 C ATOM 2805 C GLY B 81 34.172 39.335 −21.129 1.00 34.83 C ATOM 2806 O GLY B 81 35.132 40.098 −21.022 1.00 34.83 O ATOM 2807 N GLN B 82 34.315 38.056 −21.433 1.00 65.75 N ATOM 2808 CA GLN B 82 35.634 37.455 −21.536 1.00 65.75 C ATOM 2809 C GLN B 82 36.388 37.822 −22.812 1.00 65.75 C ATOM 2810 O GLN B 82 37.295 37.107 −23.228 1.00 65.75 O ATOM 2811 CB GLN B 82 35.517 35.944 −21.420 1.00 65.75 C ATOM 2812 CG GLN B 82 35.249 35.475 −20.014 1.00 65.75 C ATOM 2813 CD GLN B 82 34.569 34.133 −19.992 1.00 65.75 C ATOM 2814 OE1 GLN B 82 33.359 34.036 −20.197 1.00 65.75 O ATOM 2815 NE2 GLN B 82 35.343 33.082 −19.749 1.00 65.75 N ATOM 2816 N SER B 83 36.028 38.938 −23.428 1.00 18.01 N ATOM 2817 CA SER B 83 36.686 39.330 −24.659 1.00 18.01 C ATOM 2818 C SER B 83 37.541 40.551 −24.379 1.00 18.01 C ATOM 2819 O SER B 83 37.302 41.265 −23.409 1.00 18.01 O ATOM 2820 CB SER B 83 35.653 39.585 −25.762 1.00 18.01 C ATOM 2821 OG SER B 83 34.997 38.380 −26.139 1.00 18.01 O ATOM 2822 N GLU B 84 38.547 40.777 −25.216 1.00 35.58 N ATOM 2823 CA GLU B 84 39.490 41.866 −24.994 1.00 35.58 C ATOM 2824 C GLU B 84 38.860 43.205 −25.317 1.00 35.58 C ATOM 2825 O GLU B 84 38.050 43.307 −26.231 1.00 35.58 O ATOM 2826 CB GLU B 84 40.746 41.667 −25.842 1.00 35.58 C ATOM 2827 CG GLU B 84 41.555 40.430 −25.465 1.00 35.58 C ATOM 2828 CD GLU B 84 42.853 40.315 −26.239 1.00 35.58 C ATOM 2829 OE1 GLU B 84 42.808 40.382 −27.488 1.00 35.58 O ATOM 2830 OE2 GLU B 84 43.914 40.158 −25.591 1.00 35.58 O ATOM 2831 N GLY B 85 39.223 44.232 −24.562 1.00 30.25 N ATOM 2832 CA GLY B 85 38.678 45.550 −24.813 1.00 30.25 C ATOM 2833 C GLY B 85 38.305 46.330 −23.569 1.00 30.25 C ATOM 2834 O GLY B 85 37.677 45.799 −22.650 1.00 30.25 O ATOM 2835 N GLU B 86 38.696 47.603 −23.555 1.00 32.25 N ATOM 2836 CA GLU B 86 38.384 48.493 −22.444 1.00 32.25 C ATOM 2837 C GLU B 86 36.880 48.462 −22.220 1.00 32.25 C ATOM 2838 O GLU B 86 36.093 48.743 −23.125 1.00 32.25 O ATOM 2839 CB GLU B 86 38.894 49.918 −22.712 1.00 32.25 C ATOM 2840 CG GLU B 86 38.935 50.826 −21.478 1.00 32.25 C ATOM 2841 CD GLU B 86 39.429 52.234 −21.794 1.00 32.25 C ATOM 2842 OE1 GLU B 86 40.152 52.404 −22.799 1.00 32.25 O ATOM 2843 OE2 GLU B 86 39.093 53.170 −21.037 1.00 32.25 O ATOM 2844 N ARG B 87 36.492 48.076 −21.014 1.00 8.29 N ATOM 2845 CA ARG B 87 35.092 47.866 −20.699 1.00 8.29 C ATOM 2846 C ARG B 87 34.205 48.971 −21.260 1.00 8.29 C ATOM 2847 O ARG B 87 34.412 50.150 −20.976 1.00 8.29 O ATOM 2848 CB ARG B 87 34.881 47.749 −19.181 1.00 8.29 C ATOM 2849 CG ARG B 87 35.569 46.556 −18.507 1.00 8.29 C ATOM 2850 CD ARG B 87 35.164 45.223 −19.126 1.00 8.29 C ATOM 2851 NE ARG B 87 35.898 44.940 −20.361 1.00 8.29 N ATOM 2852 CZ ARG B 87 36.199 43.716 −20.790 1.00 8.29 C ATOM 2853 NH1 ARG B 87 35.834 42.658 −20.076 1.00 8.29 N ATOM 2854 NH2 ARG B 87 36.877 43.552 −21.924 1.00 8.29 N ATOM 2855 N MET B 88 33.221 48.567 −22.063 1.00 44.81 N ATOM 2856 CA MET B 88 32.151 49.455 −22.525 1.00 44.81 C ATOM 2857 C MET B 88 32.659 50.731 −23.185 1.00 44.81 C ATOM 2858 O MET B 88 32.226 51.829 −22.834 1.00 44.81 O ATOM 2859 CB MET B 88 31.195 49.806 −21.375 1.00 44.81 C ATOM 2860 CG MET B 88 30.734 48.602 −20.564 1.00 44.81 C ATOM 2861 SD MET B 88 29.463 48.984 −19.348 1.00 44.81 S ATOM 2862 CE MET B 88 28.070 49.254 −20.432 1.00 44.81 C ATOM 2863 N VAL B 89 33.592 50.572 −24.122 1.00 30.52 N ATOM 2864 CA VAL B 89 34.003 51.646 −25.024 1.00 30.52 C ATOM 2865 C VAL B 89 34.410 51.007 −26.340 1.00 30.52 C ATOM 2866 O VAL B 89 35.012 49.925 −26.358 1.00 30.52 O ATOM 2867 CB VAL B 89 35.178 52.487 −24.486 1.00 30.52 C ATOM 2868 CG1 VAL B 89 34.770 53.270 −23.261 1.00 30.52 C ATOM 2869 CG2 VAL B 89 36.369 51.600 −24.197 1.00 30.52 C ATOM 2870 N VAL B 90 34.081 51.682 −27.436 1.00 32.05 N ATOM 2871 CA VAL B 90 34.265 51.123 −28.765 1.00 32.05 C ATOM 2872 C VAL B 90 34.728 52.203 −29.736 1.00 32.05 C ATOM 2873 O VAL B 90 34.253 53.339 −29.683 1.00 32.05 O ATOM 2874 CB VAL B 90 32.951 50.512 −29.272 1.00 32.05 C ATOM 2875 CG1 VAL B 90 31.928 51.604 −29.517 1.00 32.05 C ATOM 2876 CG2 VAL B 90 33.187 49.680 −30.523 1.00 32.05 C ATOM 2877 N SER B 91 35.671 51.848 −30.607 1.00 55.90 N ATOM 2878 CA SER B 91 36.153 52.755 −31.644 1.00 55.90 C ATOM 2879 C SER B 91 34.985 53.362 −32.408 1.00 55.90 C ATOM 2880 O SER B 91 34.878 54.582 −32.542 1.00 55.90 O ATOM 2881 CB SER B 91 37.070 52.007 −32.610 1.00 55.90 C ATOM 2882 OG SER B 91 36.550 50.727 −32.923 1.00 55.90 O ATOM 2883 N ASP B 92 34.122 52.488 −32.918 1.00 38.77 N ATOM 2884 CA ASP B 92 32.849 52.893 −33.496 1.00 38.77 C ATOM 2885 C ASP B 92 31.811 51.785 −33.359 1.00 38.77 C ATOM 2886 O ASP B 92 32.125 50.609 −33.521 1.00 38.77 O ATOM 2887 CB ASP B 92 32.998 53.234 −34.965 1.00 38.77 C ATOM 2888 CG ASP B 92 31.664 53.390 −35.639 1.00 38.77 C ATOM 2889 OD1 ASP B 92 31.064 54.467 −35.471 1.00 38.77 O ATOM 2890 OD2 ASP B 92 31.202 52.438 −36.307 1.00 38.77 O ATOM 2891 N PHE B 93 30.569 52.167 −33.090 1.00 28.74 N ATOM 2892 CA PHE B 93 29.522 51.196 −32.797 1.00 28.74 C ATOM 2893 C PHE B 93 29.538 50.006 −33.748 1.00 28.74 C ATOM 2894 O PHE B 93 29.359 48.861 −33.327 1.00 28.74 O ATOM 2895 CB PHE B 93 28.149 51.861 −32.818 1.00 28.74 C ATOM 2896 CG PHE B 93 27.090 51.063 −32.139 1.00 28.74 C ATOM 2897 CD1 PHE B 93 27.088 50.930 −30.761 1.00 28.74 C ATOM 2898 CD2 PHE B 93 26.092 50.443 −32.871 1.00 28.74 C ATOM 2899 CE1 PHE B 93 26.110 50.183 −30.122 1.00 28.74 C ATOM 2900 CE2 PHE B 93 25.108 49.699 −32.237 1.00 28.74 C ATOM 2901 CZ PHE B 93 25.119 49.568 −30.861 1.00 28.74 C ATOM 2902 N HIS B 94 29.769 50.275 −35.029 1.00 47.32 N ATOM 2903 CA HIS B 94 29.704 49.225 −36.035 1.00 47.32 C ATOM 2904 C HIS B 94 30.618 48.070 −35.707 1.00 47.32 C ATOM 2905 O HIS B 94 30.385 46.935 −36.123 1.00 47.32 O ATOM 2906 CB HIS B 94 30.076 49.755 −37.408 1.00 47.32 C ATOM 2907 CG HIS B 94 30.297 48.674 −38.418 1.00 47.32 C ATOM 2908 ND1 HIS B 94 31.483 47.975 −38.515 1.00 47.32 N ATOM 2909 CD2 HIS B 94 29.481 48.159 −39.367 1.00 47.32 C ATOM 2910 CE1 HIS B 94 31.391 47.088 −39.489 1.00 47.32 C ATOM 2911 NE2 HIS B 94 30.185 47.176 −40.020 1.00 47.32 N ATOM 2912 N VAL B 95 31.681 48.366 −34.979 1.00 24.31 N ATOM 2913 CA VAL B 95 32.623 47.326 −34.617 1.00 24.31 C ATOM 2914 C VAL B 95 31.881 46.110 −34.069 1.00 24.31 C ATOM 2915 O VAL B 95 32.267 44.972 −34.321 1.00 24.31 O ATOM 2916 CB VAL B 95 33.644 47.814 −33.588 1.00 24.31 C ATOM 2917 CG1 VAL B 95 34.575 46.684 −33.207 1.00 24.31 C ATOM 2918 CG2 VAL B 95 34.435 48.987 −34.144 1.00 24.31 C ATOM 2919 N PHE B 96 30.812 46.345 −33.319 1.00 20.03 N ATOM 2920 CA PHE B 96 30.034 45.233 −32.803 1.00 20.03 C ATOM 2921 C PHE B 96 29.436 44.486 −33.981 1.00 20.03 C ATOM 2922 O PHE B 96 29.559 43.259 −34.103 1.00 20.03 O ATOM 2923 CB PHE B 96 28.919 45.740 −31.898 1.00 20.03 C ATOM 2924 CG PHE B 96 29.410 46.493 −30.706 1.00 20.03 C ATOM 2925 CD1 PHE B 96 30.275 45.901 −29.804 1.00 20.03 C ATOM 2926 CD2 PHE B 96 29.005 47.785 −30.478 1.00 20.03 C ATOM 2927 CE1 PHE B 96 30.730 46.589 −28.698 1.00 20.03 C ATOM 2928 CE2 PHE B 96 29.458 48.471 −29.374 1.00 20.03 C ATOM 2929 CZ PHE B 96 30.322 47.870 −28.483 1.00 20.03 C ATOM 2930 N VAL B 97 28.786 45.256 −34.850 1.00 31.01 N ATOM 2931 CA VAL B 97 28.096 44.720 −36.009 1.00 31.01 C ATOM 2932 C VAL B 97 29.029 43.837 −36.791 1.00 31.01 C ATOM 2933 O VAL B 97 28.841 42.625 −36.854 1.00 31.01 O ATOM 2934 CB VAL B 97 27.624 45.839 −36.936 1.00 31.01 C ATOM 2935 CG1 VAL B 97 27.139 45.265 −38.250 1.00 31.01 C ATOM 2936 CG2 VAL B 97 26.534 46.659 −36.265 1.00 31.01 C ATOM 2937 N ARG B 98 30.039 44.459 −37.387 1.00 39.58 N ATOM 2938 CA ARG B 98 30.999 43.740 −38.207 1.00 39.58 C ATOM 2939 C ARG B 98 31.280 42.372 −37.606 1.00 39.58 C ATOM 2940 O ARG B 98 31.073 41.343 −38.248 1.00 39.58 O ATOM 2941 CB ARG B 98 32.300 44.533 −38.308 1.00 39.58 C ATOM 2942 CG ARG B 98 33.419 43.791 −39.010 1.00 39.58 C ATOM 2943 CD ARG B 98 34.758 44.475 −38.790 1.00 39.58 C ATOM 2944 NE ARG B 98 35.151 44.479 −37.383 1.00 39.58 N ATOM 2945 CZ ARG B 98 36.003 45.348 −36.843 1.00 39.58 C ATOM 2946 NH1 ARG B 98 36.553 46.299 −37.590 1.00 39.58 N ATOM 2947 NH2 ARG B 98 36.297 45.272 −35.553 1.00 39.58 N ATOM 2948 N ASP B 99 31.725 42.389 −36.352 1.00 31.69 N ATOM 2949 CA ASP B 99 32.179 41.203 −35.637 1.00 31.69 C ATOM 2950 C ASP B 99 31.160 40.079 −35.639 1.00 31.69 C ATOM 2951 O ASP B 99 31.525 38.906 −35.720 1.00 31.69 O ATOM 2952 CB ASP B 99 32.550 41.575 −34.205 1.00 31.69 C ATOM 2953 CG ASP B 99 33.797 42.434 −34.136 1.00 31.69 C ATOM 2954 OD1 ASP B 99 34.329 42.815 −35.203 1.00 31.69 O ATOM 2955 OD2 ASP B 99 34.253 42.724 −33.013 1.00 31.69 O ATOM 2956 N VAL B 100 29.884 40.438 −35.531 1.00 33.88 N ATOM 2957 CA VAL B 100 28.816 39.455 −35.661 1.00 33.88 C ATOM 2958 C VAL B 100 28.934 38.828 −37.038 1.00 33.88 C ATOM 2959 O VAL B 100 29.153 37.626 −37.170 1.00 33.88 O ATOM 2960 CB VAL B 100 27.431 40.099 −35.502 1.00 33.88 C ATOM 2961 CG1 VAL B 100 26.342 39.033 −35.541 1.00 33.88 C ATOM 2962 CG2 VAL B 100 27.371 40.898 −34.205 1.00 33.88 C ATOM 2963 N LEU B 101 28.810 39.666 −38.059 1.00 43.71 N ATOM 2964 CA LEU B 101 28.991 39.244 −39.441 1.00 43.71 C ATOM 2965 C LEU B 101 30.215 38.356 −39.562 1.00 43.71 C ATOM 2966 O LEU B 101 30.132 37.209 −40.008 1.00 43.71 O ATOM 2967 CB LEU B 101 29.142 40.471 −40.344 1.00 43.71 C ATOM 2968 CG LEU B 101 27.839 41.193 −40.696 1.00 43.71 C ATOM 2969 CD1 LEU B 101 28.122 42.456 −41.493 1.00 43.71 C ATOM 2970 CD2 LEU B 101 26.898 40.255 −41.458 1.00 43.71 C ATOM 2971 N GLN B 102 31.350 38.920 −39.169 1.00 15.77 N ATOM 2972 CA GLN B 102 32.599 38.200 −39.071 1.00 15.77 C ATOM 2973 C GLN B 102 32.304 36.791 −38.559 1.00 15.77 C ATOM 2974 O GLN B 102 32.560 35.802 −39.245 1.00 15.77 O ATOM 2975 CB GLN B 102 33.521 38.968 −38.119 1.00 15.77 C ATOM 2976 CG GLN B 102 35.014 38.598 −38.139 1.00 15.77 C ATOM 2977 CD GLN B 102 35.892 39.663 −37.449 1.00 15.77 C ATOM 2978 OE1 GLN B 102 35.650 40.867 −37.591 1.00 15.77 O ATOM 2979 NE2 GLN B 102 36.900 39.218 −36.695 1.00 15.77 N ATOM 2980 N HIS B 103 31.715 36.700 −37.372 1.00 24.34 N ATOM 2981 CA HIS B 103 31.436 35.397 −36.757 1.00 24.34 C ATOM 2982 C HIS B 103 30.449 34.579 −37.592 1.00 24.34 C ATOM 2983 O HIS B 103 30.623 33.371 −37.790 1.00 24.34 O ATOM 2984 CB HIS B 103 30.907 35.582 −35.331 1.00 24.34 C ATOM 2985 CG HIS B 103 30.939 34.336 −34.508 1.00 24.34 C ATOM 2986 ND1 HIS B 103 31.396 34.314 −33.210 1.00 24.34 N ATOM 2987 CD2 HIS B 103 30.576 33.066 −34.800 1.00 24.34 C ATOM 2988 CE1 HIS B 103 31.307 33.086 −32.734 1.00 24.34 C ATOM 2989 NE2 HIS B 103 30.809 32.310 −33.678 1.00 24.34 N ATOM 2990 N VAL B 104 29.420 35.252 −38.087 1.00 34.72 N ATOM 2991 CA VAL B 104 28.397 34.598 −38.877 1.00 34.72 C ATOM 2992 C VAL B 104 29.011 33.930 −40.109 1.00 34.72 C ATOM 2993 O VAL B 104 29.141 32.706 −40.153 1.00 34.72 O ATOM 2994 CB VAL B 104 27.305 35.600 −39.286 1.00 34.72 C ATOM 2995 CG1 VAL B 104 26.094 34.874 −39.855 1.00 34.72 C ATOM 2996 CG2 VAL B 104 26.891 36.424 −38.085 1.00 34.72 C ATOM 2997 N ASP B 105 29.393 34.738 −41.097 1.00 51.08 N ATOM 2998 CA ASP B 105 30.033 34.241 −42.317 1.00 51.08 C ATOM 2999 C ASP B 105 30.880 33.016 −42.035 1.00 51.08 C ATOM 3000 O ASP B 105 30.847 32.026 −42.770 1.00 51.08 O ATOM 3001 CB ASP B 105 30.945 35.311 −42.905 1.00 51.08 C ATOM 3002 CG ASP B 105 30.195 36.540 −43.319 1.00 51.08 C ATOM 3003 OD1 ASP B 105 29.198 36.395 −44.048 1.00 51.08 O ATOM 3004 OD2 ASP B 105 30.608 37.647 −42.922 1.00 51.08 O ATOM 3005 N SER B 106 31.656 33.109 −40.963 1.00 28.91 N ATOM 3006 CA SER B 106 32.565 32.049 −40.574 1.00 28.91 C ATOM 3007 C SER B 106 31.823 30.755 −40.256 1.00 28.91 C ATOM 3008 O SER B 106 32.037 29.724 −40.895 1.00 28.91 O ATOM 3009 CB SER B 106 33.376 32.513 −39.372 1.00 28.91 C ATOM 3010 OG SER B 106 33.891 33.810 −39.618 1.00 28.91 O ATOM 3011 N MET B 107 30.957 30.816 −39.255 1.00 51.33 N ATOM 3012 CA MET B 107 30.108 29.688 −38.918 1.00 51.33 C ATOM 3013 C MET B 107 29.338 29.279 −40.162 1.00 51.33 C ATOM 3014 O MET B 107 29.057 28.095 −40.392 1.00 51.33 O ATOM 3015 CB MET B 107 29.125 30.104 −37.827 1.00 51.33 C ATOM 3016 CG MET B 107 28.265 28.983 −37.306 1.00 51.33 C ATOM 3017 SD MET B 107 29.280 27.839 −36.370 1.00 51.33 S ATOM 3018 CE MET B 107 30.393 28.986 −35.565 1.00 51.33 C ATOM 3019 N GLN B 108 29.015 30.289 −40.964 1.00 36.16 N ATOM 3020 CA GLN B 108 28.147 30.123 −42.116 1.00 36.16 C ATOM 3021 C GLN B 108 28.798 29.204 −43.141 1.00 36.16 C ATOM 3022 O GLN B 108 28.156 28.299 −43.673 1.00 36.16 O ATOM 3023 CB GLN B 108 27.784 31.490 −42.714 1.00 36.16 C ATOM 3024 CG GLN B 108 26.671 31.441 −43.760 1.00 36.16 C ATOM 3025 CD GLN B 108 25.474 30.603 −43.321 1.00 36.16 C ATOM 3026 OE1 GLN B 108 25.352 30.241 −42.151 1.00 36.16 O ATOM 3027 NE2 GLN B 108 24.585 30.290 −44.266 1.00 36.16 N ATOM 3028 N LYS B 109 30.080 29.436 −43.399 1.00 95.60 N ATOM 3029 CA LYS B 109 30.875 28.507 −44.183 1.00 95.60 C ATOM 3030 C LYS B 109 30.658 27.097 −43.673 1.00 95.60 C ATOM 3031 O LYS B 109 30.194 26.224 −44.405 1.00 95.60 O ATOM 3032 CB LYS B 109 32.361 28.829 −44.047 1.00 95.60 C ATOM 3033 CG LYS B 109 33.265 27.588 −44.123 1.00 95.60 C ATOM 3034 CD LYS B 109 33.424 27.068 −45.552 1.00 95.60 C ATOM 3035 CE LYS B 109 34.711 27.568 −46.206 1.00 95.60 C ATOM 3036 NZ LYS B 109 35.047 28.984 −45.872 1.00 95.60 N ATOM 3037 N ASP B 110 31.017 26.885 −42.409 1.00 48.87 N ATOM 3038 CA ASP B 110 30.979 25.564 −41.808 1.00 48.87 C ATOM 3039 C ASP B 110 29.627 24.932 −41.994 1.00 48.87 C ATOM 3040 O ASP B 110 29.482 23.719 −41.870 1.00 48.87 O ATOM 3041 CB ASP B 110 31.295 25.640 −40.321 1.00 48.87 C ATOM 3042 CG ASP B 110 32.773 25.735 −40.051 1.00 48.87 C ATOM 3043 OD1 ASP B 110 33.481 26.358 −40.870 1.00 48.87 O ATOM 3044 OD2 ASP B 110 33.221 25.185 −39.022 1.00 48.87 O ATOM 3045 N TYR B 111 28.627 25.754 −42.279 1.00 23.68 N ATOM 3046 CA TYR B 111 27.306 25.213 −42.513 1.00 23.68 C ATOM 3047 C TYR B 111 26.637 25.888 −43.685 1.00 23.68 C ATOM 3048 O TYR B 111 25.691 26.654 −43.522 1.00 23.68 O ATOM 3049 CB TYR B 111 26.465 25.302 −41.252 1.00 23.68 C ATOM 3050 CG TYR B 111 27.102 24.575 −40.094 1.00 23.68 C ATOM 3051 CD1 TYR B 111 27.975 25.232 −39.232 1.00 23.68 C ATOM 3052 CD2 TYR B 111 26.854 23.227 −39.875 1.00 23.68 C ATOM 3053 CE1 TYR B 111 28.567 24.575 −38.171 1.00 23.68 C ATOM 3054 CE2 TYR B 111 27.443 22.555 −38.813 1.00 23.68 C ATOM 3055 CZ TYR B 111 28.302 23.236 −37.962 1.00 23.68 C ATOM 3056 OH TYR B 111 28.898 22.585 −36.896 1.00 23.68 O ATOM 3057 N PRO B 112 27.120 25.572 −44.891 1.00 59.74 N ATOM 3058 CA PRO B 112 26.626 26.194 −46.118 1.00 59.74 C ATOM 3059 C PRO B 112 25.207 25.729 −46.381 1.00 59.74 C ATOM 3060 O PRO B 112 24.781 24.703 −45.846 1.00 59.74 O ATOM 3061 CB PRO B 112 27.560 25.637 −47.201 1.00 59.74 C ATOM 3062 CG PRO B 112 28.606 24.811 −46.480 1.00 59.74 C ATOM 3063 CD PRO B 112 28.005 24.432 −45.173 1.00 59.74 C ATOM 3064 N GLY B 113 24.478 26.478 −47.195 1.00 38.88 N ATOM 3065 CA GLY B 113 23.113 26.114 −47.502 1.00 38.88 C ATOM 3066 C GLY B 113 22.334 25.875 −46.227 1.00 38.88 C ATOM 3067 O GLY B 113 21.276 25.242 −46.247 1.00 38.88 O ATOM 3068 N LEU B 114 22.865 26.373 −45.111 1.00 17.76 N ATOM 3069 CA LEU B 114 22.144 26.345 −43.843 1.00 17.76 C ATOM 3070 C LEU B 114 21.654 27.753 −43.501 1.00 17.76 C ATOM 3071 O LEU B 114 22.402 28.723 −43.636 1.00 17.76 O ATOM 3072 CB LEU B 114 23.023 25.772 −42.730 1.00 17.76 C ATOM 3073 CG LEU B 114 22.290 24.989 −41.633 1.00 17.76 C ATOM 3074 CD1 LEU B 114 21.337 23.974 −42.215 1.00 17.76 C ATOM 3075 CD2 LEU B 114 23.284 24.302 −40.725 1.00 17.76 C ATOM 3076 N PRO B 115 20.384 27.868 −43.085 1.00 35.71 N ATOM 3077 CA PRO B 115 19.705 29.143 −42.819 1.00 35.71 C ATOM 3078 C PRO B 115 20.208 29.803 −41.547 1.00 35.71 C ATOM 3079 O PRO B 115 20.671 29.112 −40.638 1.00 35.71 O ATOM 3080 CB PRO B 115 18.243 28.731 −42.629 1.00 35.71 C ATOM 3081 CG PRO B 115 18.151 27.322 −43.134 1.00 35.71 C ATOM 3082 CD PRO B 115 19.486 26.724 −42.883 1.00 35.71 C ATOM 3083 N VAL B 116 20.091 31.124 −41.472 1.00 46.03 N ATOM 3084 CA VAL B 116 20.688 31.867 −40.368 1.00 46.03 C ATOM 3085 C VAL B 116 19.777 32.935 −39.775 1.00 46.03 C ATOM 3086 O VAL B 116 19.249 33.789 −40.486 1.00 46.03 O ATOM 3087 CB VAL B 116 21.988 32.548 −40.809 1.00 46.03 C ATOM 3088 CG1 VAL B 116 21.747 33.357 −42.085 1.00 46.03 C ATOM 3089 CG2 VAL B 116 22.536 33.428 −39.696 1.00 46.03 C ATOM 3090 N PHE B 117 19.633 32.887 −38.454 1.00 13.49 N ATOM 3091 CA PHE B 117 18.808 33.833 −37.705 1.00 13.49 C ATOM 3092 C PHE B 117 19.629 34.810 −36.868 1.00 13.49 C ATOM 3093 O PHE B 117 20.855 34.807 −36.910 1.00 13.49 O ATOM 3094 CB PHE B 117 17.861 33.074 −36.774 1.00 13.49 C ATOM 3095 CG PHE B 117 16.833 32.232 −37.494 1.00 13.49 C ATOM 3096 CD1 PHE B 117 17.160 30.965 −37.974 1.00 13.49 C ATOM 3097 CD2 PHE B 117 15.538 32.705 −37.681 1.00 13.49 C ATOM 3098 CE1 PHE B 117 16.214 30.196 −38.626 1.00 13.49 C ATOM 3099 CE2 PHE B 117 14.592 31.938 −38.329 1.00 13.49 C ATOM 3100 CZ PHE B 117 14.929 30.686 −38.800 1.00 13.49 C ATOM 3101 N LEU B 118 18.930 35.638 −36.102 1.00 9.00 N ATOM 3102 CA LEU B 118 19.550 36.599 −35.199 1.00 9.00 C ATOM 3103 C LEU B 118 18.683 36.774 −33.960 1.00 9.00 C ATOM 3104 O LEU B 118 17.463 36.727 −34.044 1.00 9.00 O ATOM 3105 CB LEU B 118 19.726 37.952 −35.893 1.00 9.00 C ATOM 3106 CG LEU B 118 20.933 38.088 −36.821 1.00 9.00 C ATOM 3107 CD1 LEU B 118 21.057 39.514 −37.359 1.00 9.00 C ATOM 3108 CD2 LEU B 118 22.201 37.676 −36.083 1.00 9.00 C ATOM 3109 N LEU B 119 19.313 36.977 −32.810 1.00 9.66 N ATOM 3110 CA LEU B 119 18.578 37.262 −31.586 1.00 9.66 C ATOM 3111 C LEU B 119 19.371 38.252 −30.779 1.00 9.66 C ATOM 3112 O LEU B 119 20.548 38.043 −30.526 1.00 9.66 O ATOM 3113 CB LEU B 119 18.352 35.982 −30.776 1.00 9.66 C ATOM 3114 CG LEU B 119 17.408 35.996 −29.562 1.00 9.66 C ATOM 3115 CD1 LEU B 119 16.901 34.589 −29.273 1.00 9.66 C ATOM 3116 CD2 LEU B 119 18.035 36.607 −28.302 1.00 9.66 C ATOM 3117 N GLY B 120 18.734 39.340 −30.382 1.00 9.92 N ATOM 3118 CA GLY B 120 19.412 40.321 −29.564 1.00 9.92 C ATOM 3119 C GLY B 120 18.519 40.871 −28.480 1.00 9.92 C ATOM 3120 O GLY B 120 17.301 40.756 −28.551 1.00 9.92 O ATOM 3121 N HIS B 121 19.125 41.469 −27.467 1.00 8.29 N ATOM 3122 CA HIS B 121 18.351 42.127 −26.436 1.00 8.29 C ATOM 3123 C HIS B 121 18.852 43.556 −26.280 1.00 8.29 C ATOM 3124 O HIS B 121 20.058 43.802 −26.337 1.00 8.29 O ATOM 3125 CB HIS B 121 18.446 41.365 −25.118 1.00 8.29 C ATOM 3126 CG HIS B 121 17.877 42.109 −23.958 1.00 8.29 C ATOM 3127 ND1 HIS B 121 16.791 42.945 −24.078 1.00 8.29 N ATOM 3128 CD2 HIS B 121 18.235 42.141 −22.654 1.00 8.29 C ATOM 3129 CE1 HIS B 121 16.502 43.457 −22.896 1.00 8.29 C ATOM 3130 NE2 HIS B 121 17.363 42.983 −22.014 1.00 8.29 N ATOM 3131 N SER B 122 17.916 44.489 −26.110 1.00 29.72 N ATOM 3132 CA SER B 122 18.220 45.919 −25.997 1.00 29.72 C ATOM 3133 C SER B 122 19.274 46.416 −26.987 1.00 29.72 C ATOM 3134 O SER B 122 18.986 46.548 −28.170 1.00 29.72 O ATOM 3135 CB SER B 122 18.603 46.268 −24.564 1.00 29.72 C ATOM 3136 OG SER B 122 19.270 45.180 −23.961 1.00 29.72 O ATOM 3137 N MET B 123 20.478 46.709 −26.500 1.00 15.91 N ATOM 3138 CA MET B 123 21.566 47.129 −27.374 1.00 15.91 C ATOM 3139 C MET B 123 22.055 45.958 −28.227 1.00 15.91 C ATOM 3140 O MET B 123 22.630 46.145 −29.297 1.00 15.91 O ATOM 3141 CB MET B 123 22.727 47.725 −26.572 1.00 15.91 C ATOM 3142 CG MET B 123 23.831 48.331 −27.457 1.00 15.91 C ATOM 3143 SD MET B 123 25.530 48.322 −26.796 1.00 15.91 S ATOM 3144 CE MET B 123 25.937 46.571 −26.840 1.00 15.91 C ATOM 3145 N GLY B 124 21.841 44.744 −27.742 1.00 20.90 N ATOM 3146 CA GLY B 124 22.093 43.568 −28.552 1.00 20.90 C ATOM 3147 C GLY B 124 21.172 43.614 −29.752 1.00 20.90 C ATOM 3148 O GLY B 124 21.591 43.400 −30.884 1.00 20.90 O ATOM 3149 N GLY B 125 19.906 43.905 −29.496 1.00 21.53 N ATOM 3150 CA GLY B 125 18.956 44.116 −30.564 1.00 21.53 C ATOM 3151 C GLY B 125 19.464 45.126 −31.577 1.00 21.53 C ATOM 3152 O GLY B 125 19.764 44.760 −32.715 1.00 21.53 O ATOM 3153 N ALA B 126 19.555 46.395 −31.170 1.00 5.89 N ATOM 3154 CA ALA B 126 20.064 47.461 −32.028 1.00 5.89 C ATOM 3155 C ALA B 126 21.101 46.908 −33.006 1.00 5.89 C ATOM 3156 O ALA B 126 20.951 47.003 −34.228 1.00 5.89 O ATOM 3157 CB ALA B 126 20.657 48.564 −31.181 1.00 5.89 C ATOM 3158 N ILE B 127 22.139 46.297 −32.453 1.00 28.20 N ATOM 3159 CA ILE B 127 23.154 45.643 −33.257 1.00 28.20 C ATOM 3160 C ILE B 127 22.528 44.710 −34.300 1.00 28.20 C ATOM 3161 O ILE B 127 22.578 44.991 −35.502 1.00 28.20 O ATOM 3162 CB ILE B 127 24.136 44.870 −32.365 1.00 28.20 C ATOM 3163 CG1 ILE B 127 24.930 45.849 −31.496 1.00 28.20 C ATOM 3164 CG2 ILE B 127 25.068 44.013 −33.208 1.00 28.20 C ATOM 3165 CD1 ILE B 127 25.697 45.197 −30.385 1.00 28.20 C ATOM 3166 N ALA B 128 21.940 43.610 −33.836 1.00 44.25 N ATOM 3167 CA ALA B 128 21.278 42.658 −34.720 1.00 44.25 C ATOM 3168 C ALA B 128 20.514 43.388 −35.820 1.00 44.25 C ATOM 3169 O ALA B 128 20.668 43.095 −37.009 1.00 44.25 O ATOM 3170 CB ALA B 128 20.340 41.772 −33.927 1.00 44.25 C ATOM 3171 N ILE B 129 19.696 44.350 −35.410 1.00 12.94 N ATOM 3172 CA ILE B 129 18.936 45.153 −36.357 1.00 12.94 C ATOM 3173 C ILE B 129 19.858 45.694 −37.422 1.00 12.94 C ATOM 3174 O ILE B 129 19.710 45.377 −38.597 1.00 12.94 O ATOM 3175 CB ILE B 129 18.220 46.332 −35.663 1.00 12.94 C ATOM 3176 CG1 ILE B 129 16.882 45.864 −35.080 1.00 12.94 C ATOM 3177 CG2 ILE B 129 17.984 47.468 −36.643 1.00 12.94 C ATOM 3178 CD1 ILE B 129 16.095 46.949 −34.391 1.00 12.94 C ATOM 3179 N LEU B 130 20.823 46.499 −36.991 1.00 9.12 N ATOM 3180 CA LEU B 130 21.732 47.161 −37.911 1.00 9.12 C ATOM 3181 C LEU B 130 22.527 46.165 −38.747 1.00 9.12 C ATOM 3182 O LEU B 130 23.051 46.503 −39.814 1.00 9.12 O ATOM 3183 CB LEU B 130 22.669 48.090 −37.148 1.00 9.12 C ATOM 3184 CG LEU B 130 22.003 49.359 −36.618 1.00 9.12 C ATOM 3185 CD1 LEU B 130 23.051 50.405 −36.333 1.00 9.12 C ATOM 3186 CD2 LEU B 130 20.983 49.893 −37.614 1.00 9.12 C ATOM 3187 N THR B 131 22.612 44.932 −38.265 1.00 7.55 N ATOM 3188 CA THR B 131 23.348 43.910 −38.983 1.00 7.55 C ATOM 3189 C THR B 131 22.569 43.406 −40.178 1.00 7.55 C ATOM 3190 O THR B 131 23.145 42.902 −41.132 1.00 7.55 O ATOM 3191 CB THR B 131 23.668 42.726 −38.093 1.00 7.55 C ATOM 3192 OG1 THR B 131 24.461 43.169 −36.989 1.00 7.55 O ATOM 3193 CG2 THR B 131 24.451 41.691 −38.872 1.00 7.55 C ATOM 3194 N ALA B 132 21.251 43.532 −40.126 1.00 20.48 N ATOM 3195 CA ALA B 132 20.427 43.114 −41.249 1.00 20.48 C ATOM 3196 C ALA B 132 20.432 44.201 −42.319 1.00 20.48 C ATOM 3197 O ALA B 132 20.263 43.927 −43.505 1.00 20.48 O ATOM 3198 CB ALA B 132 19.014 42.805 −40.783 1.00 20.48 C ATOM 3199 N ALA B 133 20.634 45.437 −41.881 1.00 63.90 N ATOM 3200 CA ALA B 133 20.759 46.566 −42.787 1.00 63.90 C ATOM 3201 C ALA B 133 21.858 46.299 −43.808 1.00 63.90 C ATOM 3202 O ALA B 133 21.824 46.807 −44.926 1.00 63.90 O ATOM 3203 CB ALA B 133 21.065 47.834 −41.999 1.00 63.90 C ATOM 3204 N GLU B 134 22.833 45.490 −43.421 1.00 30.80 N ATOM 3205 CA GLU B 134 23.993 45.251 −44.265 1.00 30.80 C ATOM 3206 C GLU B 134 23.857 44.019 −45.167 1.00 30.80 C ATOM 3207 O GLU B 134 24.380 44.004 −46.283 1.00 30.80 O ATOM 3208 CB GLU B 134 25.236 45.144 −43.392 1.00 30.80 C ATOM 3209 CG GLU B 134 26.507 44.838 −44.141 1.00 30.80 C ATOM 3210 CD GLU B 134 27.717 45.309 −43.379 1.00 30.80 C ATOM 3211 OE1 GLU B 134 27.520 46.059 −42.396 1.00 30.80 O ATOM 3212 OE2 GLU B 134 28.850 44.940 −43.758 1.00 30.80 O ATOM 3213 N ARG B 135 23.160 42.991 −44.685 1.00 20.92 N ATOM 3214 CA ARG B 135 22.911 41.787 −45.484 1.00 20.92 C ATOM 3215 C ARG B 135 21.426 41.604 −45.799 1.00 20.92 C ATOM 3216 O ARG B 135 20.828 40.596 −45.434 1.00 20.92 O ATOM 3217 CB ARG B 135 23.447 40.533 −44.787 1.00 20.92 C ATOM 3218 CG ARG B 135 24.897 40.635 −44.339 1.00 20.92 C ATOM 3219 CD ARG B 135 25.882 40.234 −45.438 1.00 20.92 C ATOM 3220 NE ARG B 135 27.201 40.849 −45.254 1.00 20.92 N ATOM 3221 CZ ARG B 135 28.254 40.250 −44.704 1.00 20.92 C ATOM 3222 NH1 ARG B 135 28.165 39.000 −44.275 1.00 20.92 N ATOM 3223 NH2 ARG B 135 29.402 40.903 −44.585 1.00 20.92 N ATOM 3224 N PRO B 136 20.828 42.581 −46.490 1.00 35.39 N ATOM 3225 CA PRO B 136 19.434 42.433 −46.909 1.00 35.39 C ATOM 3226 C PRO B 136 19.184 41.110 −47.626 1.00 35.39 C ATOM 3227 O PRO B 136 19.721 40.880 −48.712 1.00 35.39 O ATOM 3228 CB PRO B 136 19.249 43.581 −47.899 1.00 35.39 C ATOM 3229 CG PRO B 136 20.247 44.599 −47.487 1.00 35.39 C ATOM 3230 CD PRO B 136 21.421 43.842 −46.969 1.00 35.39 C ATOM 3231 N GLY B 137 18.370 40.252 −47.028 1.00 41.34 N ATOM 3232 CA GLY B 137 17.966 39.031 −47.691 1.00 41.34 C ATOM 3233 C GLY B 137 18.827 37.849 −47.319 1.00 41.34 C ATOM 3234 O GLY B 137 18.583 36.722 −47.756 1.00 41.34 O ATOM 3235 N HIS B 138 19.841 38.090 −46.502 1.00 51.70 N ATOM 3236 CA HIS B 138 20.677 36.991 −46.051 1.00 51.70 C ATOM 3237 C HIS B 138 19.990 36.196 −44.941 1.00 51.70 C ATOM 3238 O HIS B 138 19.841 34.974 −45.035 1.00 51.70 O ATOM 3239 CB HIS B 138 22.029 37.506 −45.570 1.00 51.70 C ATOM 3240 CG HIS B 138 23.049 36.431 −45.396 1.00 51.70 C ATOM 3241 ND1 HIS B 138 24.356 36.572 −45.809 1.00 51.70 N ATOM 3242 CD2 HIS B 138 22.953 35.187 −44.870 1.00 51.70 C ATOM 3243 CE1 HIS B 138 25.025 35.469 −45.527 1.00 51.70 C ATOM 3244 NE2 HIS B 138 24.196 34.611 −44.957 1.00 51.70 N ATOM 3245 N PHE B 139 19.564 36.900 −43.897 1.00 39.37 N ATOM 3246 CA PHE B 139 19.043 36.255 −42.698 1.00 39.37 C ATOM 3247 C PHE B 139 17.611 35.764 −42.830 1.00 39.37 C ATOM 3248 O PHE B 139 16.748 36.459 −43.369 1.00 39.37 O ATOM 3249 CB PHE B 139 19.125 37.201 −41.511 1.00 39.37 C ATOM 3250 CG PHE B 139 20.503 37.687 −41.227 1.00 39.37 C ATOM 3251 CD1 PHE B 139 21.486 36.804 −40.808 1.00 39.37 C ATOM 3252 CD2 PHE B 139 20.816 39.035 −41.363 1.00 39.37 C ATOM 3253 CE1 PHE B 139 22.754 37.250 −40.539 1.00 39.37 C ATOM 3254 CE2 PHE B 139 22.089 39.490 −41.092 1.00 39.37 C ATOM 3255 CZ PHE B 139 23.059 38.596 −40.678 1.00 39.37 C ATOM 3256 N ALA B 140 17.369 34.570 −42.296 1.00 19.08 N ATOM 3257 CA ALA B 140 16.051 33.951 −42.314 1.00 19.08 C ATOM 3258 C ALA B 140 15.059 34.708 −41.440 1.00 19.08 C ATOM 3259 O ALA B 140 13.862 34.758 −41.739 1.00 19.08 O ATOM 3260 CB ALA B 140 16.154 32.505 −41.871 1.00 19.08 C ATOM 3261 N GLY B 141 15.557 35.301 −40.362 1.00 42.69 N ATOM 3262 CA GLY B 141 14.708 36.062 −39.468 1.00 42.69 C ATOM 3263 C GLY B 141 15.413 36.424 −38.182 1.00 42.69 C ATOM 3264 O GLY B 141 16.366 35.759 −37.793 1.00 42.69 O ATOM 3265 N MET B 142 14.948 37.481 −37.525 1.00 13.96 N ATOM 3266 CA MET B 142 15.551 37.904 −36.265 1.00 13.96 C ATOM 3267 C MET B 142 14.543 38.115 −35.113 1.00 13.96 C ATOM 3268 O MET B 142 13.556 38.843 −35.252 1.00 13.96 O ATOM 3269 CB MET B 142 16.380 39.164 −36.484 1.00 13.96 C ATOM 3270 CG MET B 142 15.555 40.340 −36.906 1.00 13.96 C ATOM 3271 SD MET B 142 16.487 41.865 −36.849 1.00 13.96 S ATOM 3272 CE MET B 142 15.255 43.045 −37.367 1.00 13.96 C ATOM 3273 N VAL B 143 14.808 37.463 −33.982 1.00 9.64 N ATOM 3274 CA VAL B 143 14.000 37.608 −32.777 1.00 9.64 C ATOM 3275 C VAL B 143 14.614 38.702 −31.952 1.00 9.64 C ATOM 3276 O VAL B 143 15.803 38.671 −31.684 1.00 9.64 O ATOM 3277 CB VAL B 143 14.024 36.322 −31.928 1.00 9.64 C ATOM 3278 CG1 VAL B 143 13.584 36.603 −30.495 1.00 9.64 C ATOM 3279 CG2 VAL B 143 13.157 35.248 −32.561 1.00 9.64 C ATOM 3280 N LEU B 144 13.811 39.664 −31.534 1.00 7.48 N ATOM 3281 CA LEU B 144 14.336 40.805 −30.809 1.00 7.48 C ATOM 3282 C LEU B 144 13.617 40.981 −29.487 1.00 7.48 C ATOM 3283 O LEU B 144 12.407 41.162 −29.459 1.00 7.48 O ATOM 3284 CB LEU B 144 14.165 42.061 −31.653 1.00 7.48 C ATOM 3285 CG LEU B 144 15.100 42.166 −32.851 1.00 7.48 C ATOM 3286 CD1 LEU B 144 14.402 42.815 −34.034 1.00 7.48 C ATOM 3287 CD2 LEU B 144 16.333 42.939 −32.461 1.00 7.48 C ATOM 3288 N ILE B 145 14.359 40.934 −28.388 1.00 10.58 N ATOM 3289 CA ILE B 145 13.770 41.165 −27.076 1.00 10.58 C ATOM 3290 C ILE B 145 14.021 42.593 −26.630 1.00 10.58 C ATOM 3291 O ILE B 145 15.154 42.988 −26.362 1.00 10.58 O ATOM 3292 CB ILE B 145 14.314 40.189 −26.025 1.00 10.58 C ATOM 3293 CG1 ILE B 145 14.116 38.742 −26.496 1.00 10.58 C ATOM 3294 CG2 ILE B 145 13.631 40.415 −24.682 1.00 10.58 C ATOM 3295 CD1 ILE B 145 15.130 37.757 −25.935 1.00 10.58 C ATOM 3296 N SER B 146 12.937 43.354 −26.550 1.00 4.00 N ATOM 3297 CA SER B 146 12.983 44.779 −26.252 1.00 4.00 C ATOM 3298 C SER B 146 14.317 45.385 −26.646 1.00 4.00 C ATOM 3299 O SER B 146 15.038 45.876 −25.784 1.00 4.00 O ATOM 3300 CB SER B 146 12.670 45.054 −24.772 1.00 4.00 C ATOM 3301 OG SER B 146 13.624 44.480 −23.907 1.00 4.00 O ATOM 3302 N PRO B 147 14.645 45.345 −27.955 1.00 4.57 N ATOM 3303 CA PRO B 147 15.849 45.980 −28.494 1.00 4.57 C ATOM 3304 C PRO B 147 15.862 47.480 −28.251 1.00 4.57 C ATOM 3305 O PRO B 147 14.827 48.084 −27.943 1.00 4.57 O ATOM 3306 CB PRO B 147 15.732 45.708 −29.998 1.00 4.57 C ATOM 3307 CG PRO B 147 14.289 45.487 −30.219 1.00 4.57 C ATOM 3308 CD PRO B 147 13.903 44.671 −29.032 1.00 4.57 C ATOM 3309 N LEU B 148 17.045 48.064 −28.398 1.00 35.27 N ATOM 3310 CA LEU B 148 17.235 49.499 −28.235 1.00 35.27 C ATOM 3311 C LEU B 148 16.942 50.238 −29.523 1.00 35.27 C ATOM 3312 O LEU B 148 17.827 50.458 −30.348 1.00 35.27 O ATOM 3313 CB LEU B 148 18.663 49.811 −27.804 1.00 35.27 C ATOM 3314 CG LEU B 148 19.039 51.286 −27.916 1.00 35.27 C ATOM 3315 CD1 LEU B 148 18.097 52.136 −27.080 1.00 35.27 C ATOM 3316 CD2 LEU B 148 20.483 51.502 −27.509 1.00 35.27 C ATOM 3317 N VAL B 149 15.689 50.616 −29.693 1.00 18.02 N ATOM 3318 CA VAL B 149 15.307 51.408 −30.833 1.00 18.02 C ATOM 3319 C VAL B 149 15.329 52.850 −30.374 1.00 18.02 C ATOM 3320 O VAL B 149 16.185 53.634 −30.777 1.00 18.02 O ATOM 3321 CB VAL B 149 13.913 51.009 −31.313 1.00 18.02 C ATOM 3322 CG1 VAL B 149 13.432 51.944 −32.390 1.00 18.02 C ATOM 3323 CG2 VAL B 149 13.948 49.597 −31.841 1.00 18.02 C ATOM 3324 N LEU B 150 14.376 53.182 −29.514 1.00 17.90 N ATOM 3325 CA LEU B 150 14.356 54.445 −28.799 1.00 17.90 C ATOM 3326 C LEU B 150 14.478 54.108 −27.325 1.00 17.90 C ATOM 3327 O LEU B 150 13.909 53.112 −26.866 1.00 17.90 O ATOM 3328 CB LEU B 150 13.027 55.146 −29.027 1.00 17.90 C ATOM 3329 CG LEU B 150 12.827 55.923 −30.321 1.00 17.90 C ATOM 3330 CD1 LEU B 150 13.875 55.588 −31.364 1.00 17.90 C ATOM 3331 CD2 LEU B 150 11.427 55.671 −30.838 1.00 17.90 C ATOM 3332 N ALA B 151 15.206 54.931 −26.581 1.00 30.48 N ATOM 3333 CA ALA B 151 15.391 54.684 −25.157 1.00 30.48 C ATOM 3334 C ALA B 151 14.616 55.675 −24.297 1.00 30.48 C ATOM 3335 O ALA B 151 14.440 56.831 −24.685 1.00 30.48 O ATOM 3336 CB ALA B 151 16.859 54.724 −24.804 1.00 30.48 C ATOM 3337 N ASN B 152 14.148 55.205 −23.140 1.00 28.74 N ATOM 3338 CA ASN B 152 13.562 56.066 −22.119 1.00 28.74 C ATOM 3339 C ASN B 152 14.180 57.436 −22.286 1.00 28.74 C ATOM 3340 O ASN B 152 15.367 57.536 −22.587 1.00 28.74 O ATOM 3341 CB ASN B 152 13.880 55.523 −20.727 1.00 28.74 C ATOM 3342 CG ASN B 152 12.843 55.912 −19.690 1.00 28.74 C ATOM 3343 OD1 ASN B 152 13.183 56.285 −18.567 1.00 28.74 O ATOM 3344 ND2 ASN B 152 11.569 55.810 −20.056 1.00 28.74 N ATOM 3345 N PRO B 153 13.378 58.497 −22.111 1.00 80.10 N ATOM 3346 CA PRO B 153 13.790 59.853 −22.494 1.00 80.10 C ATOM 3347 C PRO B 153 14.575 60.669 −21.476 1.00 80.10 C ATOM 3348 O PRO B 153 14.023 61.594 −20.868 1.00 80.10 O ATOM 3349 CB PRO B 153 12.463 60.559 −22.799 1.00 80.10 C ATOM 3350 CG PRO B 153 11.390 59.499 −22.699 1.00 80.10 C ATOM 3351 CD PRO B 153 11.942 58.435 −21.813 1.00 80.10 C ATOM 3352 N GLU B 154 15.869 60.349 −21.385 1.00 37.42 N ATOM 3353 CA GLU B 154 16.902 61.235 −20.845 1.00 37.42 C ATOM 3354 C GLU B 154 18.229 61.132 −21.615 1.00 37.42 C ATOM 3355 O GLU B 154 18.252 60.656 −22.751 1.00 37.42 O ATOM 3356 CB GLU B 154 17.109 61.031 −19.344 1.00 37.42 C ATOM 3357 CG GLU B 154 16.239 61.954 −18.463 1.00 37.42 C ATOM 3358 CD GLU B 154 16.385 63.439 −18.795 1.00 37.42 C ATOM 3359 OE1 GLU B 154 16.489 64.252 −17.851 1.00 37.42 O ATOM 3360 OE2 GLU B 154 16.394 63.796 −19.994 1.00 37.42 O ATOM 3361 N SER B 155 19.318 61.585 −20.987 1.00 30.62 N ATOM 3362 CA SER B 155 20.605 61.832 −21.666 1.00 30.62 C ATOM 3363 C SER B 155 20.479 62.232 −23.146 1.00 30.62 C ATOM 3364 O SER B 155 20.662 63.398 −23.511 1.00 30.62 O ATOM 3365 CB SER B 155 21.560 60.645 −21.511 1.00 30.62 C ATOM 3366 OG SER B 155 22.696 60.798 −22.348 1.00 30.62 O ATOM 3367 N GLY B 177 25.272 58.139 −12.645 1.00 48.88 N ATOM 3368 CA GLY B 177 24.261 57.640 −11.727 1.00 48.88 C ATOM 3369 C GLY B 177 23.635 56.350 −12.225 1.00 48.88 C ATOM 3370 O GLY B 177 22.424 56.300 −12.483 1.00 48.88 O ATOM 3371 N PRO B 178 24.466 55.296 −12.352 1.00 28.84 N ATOM 3372 CA PRO B 178 24.179 53.997 −12.973 1.00 28.84 C ATOM 3373 C PRO B 178 22.775 53.417 −12.764 1.00 28.84 C ATOM 3374 CB PRO B 178 25.241 53.083 −12.359 1.00 28.84 C ATOM 3375 CG PRO B 178 26.399 53.977 −12.175 1.00 28.84 C ATOM 3376 CD PRO B 178 25.846 55.341 −11.832 1.00 28.84 C ATOM 3377 O PRO B 178 22.239 53.352 −11.657 1.00 28.84 O ATOM 3378 N ILE B 179 22.193 53.025 −13.889 1.00 41.11 N ATOM 3379 CA ILE B 179 21.087 52.078 −13.956 1.00 41.11 C ATOM 3380 C ILE B 179 20.696 51.464 −12.610 1.00 41.11 C ATOM 3381 O ILE B 179 21.069 50.342 −12.285 1.00 41.11 O ATOM 3382 CB ILE B 179 21.433 50.948 −14.979 1.00 41.11 C ATOM 3383 CG1 ILE B 179 21.232 51.453 −16.405 1.00 41.11 C ATOM 3384 CG2 ILE B 179 20.587 49.701 −14.768 1.00 41.11 C ATOM 3385 CD1 ILE B 179 21.250 52.958 −16.526 1.00 41.11 C ATOM 3386 N ASP B 180 19.966 52.223 −11.817 1.00 21.56 N ATOM 3387 CA ASP B 180 19.186 51.659 −10.738 1.00 21.56 C ATOM 3388 C ASP B 180 18.643 50.292 −11.172 1.00 21.56 C ATOM 3389 O ASP B 180 17.696 50.208 −11.961 1.00 21.56 O ATOM 3390 CB ASP B 180 18.029 52.606 −10.439 1.00 21.56 C ATOM 3391 CG ASP B 180 17.025 52.019 −9.479 1.00 21.56 C ATOM 3392 OD1 ASP B 180 17.400 51.096 −8.729 1.00 21.56 O ATOM 3393 OD2 ASP B 180 15.864 52.485 −9.465 1.00 21.56 O ATOM 3394 N SER B 181 19.242 49.228 −10.646 1.00 32.37 N ATOM 3395 CA SER B 181 18.961 47.861 −11.083 1.00 32.37 C ATOM 3396 C SER B 181 17.498 47.444 −10.929 1.00 32.37 C ATOM 3397 O SER B 181 17.115 46.344 −11.322 1.00 32.37 O ATOM 3398 CB SER B 181 19.861 46.883 −10.324 1.00 32.37 C ATOM 3399 OG SER B 181 19.751 47.079 −8.920 1.00 32.37 O ATOM 3400 N SER B 182 16.687 48.329 −10.358 1.00 10.51 N ATOM 3401 CA SER B 182 15.279 48.041 −10.105 1.00 10.51 C ATOM 3402 C SER B 182 14.491 47.985 −11.398 1.00 10.51 C ATOM 3403 O SER B 182 13.564 47.201 −11.530 1.00 10.51 O ATOM 3404 CB SER B 182 14.682 49.111 −9.194 1.00 10.51 C ATOM 3405 OG SER B 182 15.557 49.396 −8.116 1.00 10.51 O ATOM 3406 N VAL B 183 14.885 48.819 −12.351 1.00 27.38 N ATOM 3407 CA VAL B 183 14.126 49.027 −13.576 1.00 27.38 C ATOM 3408 C VAL B 183 14.282 47.903 −14.600 1.00 27.38 C ATOM 3409 O VAL B 183 13.786 48.009 −15.722 1.00 27.38 O ATOM 3410 CB VAL B 183 14.550 50.341 −14.234 1.00 27.38 C ATOM 3411 CG1 VAL B 183 14.763 51.389 −13.171 1.00 27.38 C ATOM 3412 CG2 VAL B 183 15.832 50.141 −15.014 1.00 27.38 C ATOM 3413 N LEU B 184 14.966 46.830 −14.228 1.00 12.12 N ATOM 3414 CA LEU B 184 15.241 45.776 −15.190 1.00 12.12 C ATOM 3415 C LEU B 184 14.118 44.764 −15.222 1.00 12.12 C ATOM 3416 O LEU B 184 13.533 44.504 −16.275 1.00 12.12 O ATOM 3417 CB LEU B 184 16.559 45.066 −14.874 1.00 12.12 C ATOM 3418 CG LEU B 184 17.879 45.823 −15.034 1.00 12.12 C ATOM 3419 CD1 LEU B 184 18.919 44.910 −15.645 1.00 12.12 C ATOM 3420 CD2 LEU B 184 17.707 47.042 −15.906 1.00 12.12 C ATOM 3421 N SER B 185 13.839 44.186 −14.058 1.00 5.63 N ATOM 3422 CA SER B 185 12.843 43.126 −13.918 1.00 5.63 C ATOM 3423 C SER B 185 12.180 43.191 −12.536 1.00 5.63 C ATOM 3424 O SER B 185 12.815 43.543 −11.536 1.00 5.63 O ATOM 3425 CB SER B 185 13.484 41.749 −14.156 1.00 5.63 C ATOM 3426 OG SER B 185 12.633 40.711 −13.722 1.00 5.63 O ATOM 3427 N ARG B 186 10.895 42.866 −12.487 1.00 13.63 N ATOM 3428 CA ARG B 186 10.180 42.793 −11.228 1.00 13.63 C ATOM 3429 C ARG B 186 10.633 41.551 −10.470 1.00 13.63 C ATOM 3430 O ARG B 186 10.370 41.393 −9.273 1.00 13.63 O ATOM 3431 CB ARG B 186 8.680 42.729 −11.487 1.00 13.63 C ATOM 3432 CG ARG B 186 8.108 43.969 −12.134 1.00 13.63 C ATOM 3433 CD ARG B 186 6.630 43.785 −12.484 1.00 13.63 C ATOM 3434 NE ARG B 186 6.440 43.052 −13.735 1.00 13.63 N ATOM 3435 CZ ARG B 186 5.251 42.785 −14.272 1.00 13.63 C ATOM 3436 NH1 ARG B 186 4.145 43.192 −13.658 1.00 13.63 N ATOM 3437 NH2 ARG B 186 5.164 42.112 −15.416 1.00 13.63 N ATOM 3438 N ASN B 187 11.315 40.668 −11.187 1.00 10.43 N ATOM 3439 CA ASN B 187 11.816 39.438 −10.613 1.00 10.43 C ATOM 3440 C ASN B 187 13.075 39.716 −9.805 1.00 10.43 C ATOM 3441 O ASN B 187 14.160 39.807 −10.367 1.00 10.43 O ATOM 3442 CB ASN B 187 12.120 38.446 −11.729 1.00 10.43 C ATOM 3443 CG ASN B 187 12.608 37.123 −11.205 1.00 10.43 C ATOM 3444 OD1 ASN B 187 12.707 36.923 −9.999 1.00 10.43 O ATOM 3445 ND2 ASN B 187 12.912 36.206 −12.103 1.00 10.43 N ATOM 3446 N LYS B 188 12.938 39.856 −8.489 1.00 25.06 N ATOM 3447 CA LYS B 188 14.084 40.181 −7.642 1.00 25.06 C ATOM 3448 C LYS B 188 15.186 39.145 −7.775 1.00 25.06 C ATOM 3449 O LYS B 188 16.367 39.472 −7.746 1.00 25.06 O ATOM 3450 CB LYS B 188 13.661 40.299 −6.181 1.00 25.06 C ATOM 3451 CG LYS B 188 12.487 41.230 −5.960 1.00 25.06 C ATOM 3452 CD LYS B 188 12.421 41.736 −4.524 1.00 25.06 C ATOM 3453 CE LYS B 188 11.087 42.435 −4.264 1.00 25.06 C ATOM 3454 NZ LYS B 188 10.587 43.202 −5.458 1.00 25.06 N ATOM 3455 N THR B 189 14.789 37.889 −7.919 1.00 4.60 N ATOM 3456 CA THR B 189 15.748 36.804 −8.075 1.00 4.60 C ATOM 3457 C THR B 189 16.742 37.105 −9.195 1.00 4.60 C ATOM 3458 O THR B 189 17.950 37.071 −8.985 1.00 4.60 O ATOM 3459 CB THR B 189 15.043 35.454 −8.339 1.00 4.60 C ATOM 3460 OG1 THR B 189 14.047 35.230 −7.337 1.00 4.60 O ATOM 3461 CG2 THR B 189 16.031 34.312 −8.292 1.00 4.60 C ATOM 3462 N GLU B 190 16.221 37.405 −10.379 1.00 8.88 N ATOM 3463 CA GLU B 190 17.050 37.687 −11.540 1.00 8.88 C ATOM 3464 C GLU B 190 17.732 39.036 −11.418 1.00 8.88 C ATOM 3465 O GLU B 190 18.573 39.393 −12.247 1.00 8.88 O ATOM 3466 CB GLU B 190 16.212 37.670 −12.808 1.00 8.88 C ATOM 3467 CG GLU B 190 15.729 36.300 −13.216 1.00 8.88 C ATOM 3468 CD GLU B 190 16.834 35.413 −13.761 1.00 8.88 C ATOM 3469 OE1 GLU B 190 17.955 35.906 −13.979 1.00 8.88 O ATOM 3470 OE2 GLU B 190 16.580 34.215 −13.980 1.00 8.88 O ATOM 3471 N VAL B 191 17.365 39.782 −10.380 1.00 23.35 N ATOM 3472 CA VAL B 191 17.958 41.094 −10.122 1.00 23.35 C ATOM 3473 C VAL B 191 19.171 40.996 −9.211 1.00 23.35 C ATOM 3474 O VAL B 191 20.141 41.741 −9.364 1.00 23.35 O ATOM 3475 CB VAL B 191 16.977 42.034 −9.447 1.00 23.35 C ATOM 3476 CG1 VAL B 191 17.725 43.215 −8.887 1.00 23.35 C ATOM 3477 CG2 VAL B 191 15.917 42.478 −10.432 1.00 23.35 C ATOM 3478 N ASP B 192 19.095 40.092 −8.242 1.00 12.03 N ATOM 3479 CA ASP B 192 20.245 39.775 −7.423 1.00 12.03 C ATOM 3480 C ASP B 192 21.309 39.230 −8.348 1.00 12.03 C ATOM 3481 O ASP B 192 22.471 39.608 −8.266 1.00 12.03 O ATOM 3482 CB ASP B 192 19.879 38.704 −6.404 1.00 12.03 C ATOM 3483 CG ASP B 192 18.844 39.170 −5.426 1.00 12.03 C ATOM 3484 OD1 ASP B 192 18.678 40.404 −5.308 1.00 12.03 O ATOM 3485 OD2 ASP B 192 18.208 38.311 −4.776 1.00 12.03 O ATOM 3486 N ILE B 193 20.894 38.329 −9.230 1.00 19.54 N ATOM 3487 CA ILE B 193 21.813 37.683 −10.146 1.00 19.54 C ATOM 3488 C ILE B 193 22.556 38.732 −10.952 1.00 19.54 C ATOM 3489 O ILE B 193 23.735 38.581 −11.256 1.00 19.54 O ATOM 3490 CB ILE B 193 21.081 36.747 −11.110 1.00 19.54 C ATOM 3491 CG1 ILE B 193 20.346 35.641 −10.345 1.00 19.54 C ATOM 3492 CG2 ILE B 193 22.060 36.149 −12.097 1.00 19.54 C ATOM 3493 CD1 ILE B 193 19.233 34.987 −11.150 1.00 19.54 C ATOM 3494 N TYR B 194 21.865 39.805 −11.298 1.00 24.81 N ATOM 3495 CA TYR B 194 22.513 40.880 −12.026 1.00 24.81 C ATOM 3496 C TYR B 194 23.568 41.566 −11.170 1.00 24.81 C ATOM 3497 O TYR B 194 24.660 41.838 −11.646 1.00 24.81 O ATOM 3498 CB TYR B 194 21.496 41.906 −12.521 1.00 24.81 C ATOM 3499 CG TYR B 194 22.131 43.033 −13.295 1.00 24.81 C ATOM 3500 CD1 TYR B 194 22.350 42.924 −14.663 1.00 24.81 C ATOM 3501 CD2 TYR B 194 22.525 44.206 −12.657 1.00 24.81 C ATOM 3502 CE1 TYR B 194 22.937 43.953 −15.375 1.00 24.81 C ATOM 3503 CE2 TYR B 194 23.114 45.242 −13.367 1.00 24.81 C ATOM 3504 CZ TYR B 194 23.319 45.109 −14.724 1.00 24.81 C ATOM 3505 OH TYR B 194 23.909 46.138 −15.424 1.00 24.81 O ATOM 3506 N ASN B 195 23.242 41.840 −9.909 1.00 27.84 N ATOM 3507 CA ASN B 195 24.172 42.524 −9.003 1.00 27.84 C ATOM 3508 C ASN B 195 25.221 41.614 −8.373 1.00 27.84 C ATOM 3509 O ASN B 195 25.825 41.967 −7.372 1.00 27.84 O ATOM 3510 CB ASN B 195 23.410 43.234 −7.889 1.00 27.84 C ATOM 3511 CG ASN B 195 22.302 44.100 −8.414 1.00 27.84 C ATOM 3512 OD1 ASN B 195 21.859 43.930 −9.548 1.00 27.84 O ATOM 3513 ND2 ASN B 195 21.839 45.036 −7.593 1.00 27.84 N ATOM 3514 N SER B 196 25.432 40.442 −8.955 1.00 10.69 N ATOM 3515 CA SER B 196 26.340 39.467 −8.378 1.00 10.69 C ATOM 3516 C SER B 196 27.260 38.868 −9.435 1.00 10.69 C ATOM 3517 O SER B 196 28.367 38.431 −9.122 1.00 10.69 O ATOM 3518 CB SER B 196 25.552 38.361 −7.687 1.00 10.69 C ATOM 3519 OG SER B 196 24.840 38.856 −6.562 1.00 10.69 O ATOM 3520 N ASP B 197 26.806 38.855 −10.688 1.00 10.67 N ATOM 3521 CA ASP B 197 27.625 38.333 −11.782 1.00 10.67 C ATOM 3522 C ASP B 197 28.836 39.215 −12.074 1.00 10.67 C ATOM 3523 O ASP B 197 28.688 40.372 −12.480 1.00 10.67 O ATOM 3524 CB ASP B 197 26.793 38.152 −13.049 1.00 10.67 C ATOM 3525 CG ASP B 197 27.646 37.971 −14.280 1.00 10.67 C ATOM 3526 OD1 ASP B 197 28.824 37.577 −14.162 1.00 10.67 O ATOM 3527 OD2 ASP B 197 27.133 38.232 −15.377 1.00 10.67 O ATOM 3528 N PRO B 198 30.043 38.658 −11.891 1.00 35.07 N ATOM 3529 CA PRO B 198 31.313 39.383 −12.036 1.00 35.07 C ATOM 3530 C PRO B 198 31.469 40.095 −13.374 1.00 35.07 C ATOM 3531 O PRO B 198 32.144 41.125 −13.436 1.00 35.07 O ATOM 3532 CB PRO B 198 32.365 38.274 −11.942 1.00 35.07 C ATOM 3533 CG PRO B 198 31.698 37.168 −11.226 1.00 35.07 C ATOM 3534 CD PRO B 198 30.248 37.234 −11.582 1.00 35.07 C ATOM 3535 N LEU B 199 30.854 39.555 −14.421 1.00 19.08 N ATOM 3536 CA LEU B 199 31.152 40.000 −15.771 1.00 19.08 C ATOM 3537 C LEU B 199 30.332 41.188 −16.259 1.00 19.08 C ATOM 3538 O LEU B 199 30.555 41.677 −17.358 1.00 19.08 O ATOM 3539 CB LEU B 199 31.008 38.840 −16.751 1.00 19.08 C ATOM 3540 CG LEU B 199 31.825 37.582 −16.466 1.00 19.08 C ATOM 3541 CD1 LEU B 199 31.565 36.538 −17.537 1.00 19.08 C ATOM 3542 CD2 LEU B 199 33.299 37.917 −16.384 1.00 19.08 C ATOM 3543 N ILE B 200 29.383 41.654 −15.462 1.00 14.51 N ATOM 3544 CA ILE B 200 28.623 42.825 −15.865 1.00 14.51 C ATOM 3545 C ILE B 200 29.226 44.111 −15.348 1.00 14.51 C ATOM 3546 O ILE B 200 29.394 44.285 −14.145 1.00 14.51 O ATOM 3547 CB ILE B 200 27.150 42.762 −15.428 1.00 14.51 C ATOM 3548 CG1 ILE B 200 26.894 41.552 −14.542 1.00 14.51 C ATOM 3549 CG2 ILE B 200 26.238 42.692 −16.634 1.00 14.51 C ATOM 3550 CD1 ILE B 200 25.511 40.980 −14.702 1.00 14.51 C ATOM 3551 N CYS B 201 29.554 45.024 −16.250 1.00 38.69 N ATOM 3552 CA CYS B 201 29.944 46.336 −15.785 1.00 38.69 C ATOM 3553 C CYS B 201 28.718 47.035 −15.227 1.00 38.69 C ATOM 3554 O CYS B 201 27.838 47.445 −15.972 1.00 38.69 O ATOM 3555 CB CYS B 201 30.560 47.176 −16.895 1.00 38.69 C ATOM 3556 SG CYS B 201 31.214 48.760 −16.290 1.00 38.69 S ATOM 3557 N ARG B 202 28.646 47.141 −13.909 1.00 22.87 N ATOM 3558 CA ARG B 202 27.512 47.799 −13.269 1.00 22.87 C ATOM 3559 C ARG B 202 27.682 49.316 −13.207 1.00 22.87 C ATOM 3560 O ARG B 202 26.719 50.050 −12.979 1.00 22.87 O ATOM 3561 CB ARG B 202 27.293 47.242 −11.868 1.00 22.87 C ATOM 3562 CG ARG B 202 26.679 45.873 −11.843 1.00 22.87 C ATOM 3563 CD ARG B 202 26.801 45.310 −10.459 1.00 22.87 C ATOM 3564 NE ARG B 202 26.658 43.862 −10.455 1.00 22.87 N ATOM 3565 CZ ARG B 202 27.533 43.021 −10.996 1.00 22.87 C ATOM 3566 NH1 ARG B 202 28.610 43.471 −11.612 1.00 22.87 N ATOM 3567 NH2 ARG B 202 27.322 41.722 −10.935 1.00 22.87 N ATOM 3568 N ALA B 203 28.914 49.771 −13.396 1.00 43.28 N ATOM 3569 CA ALA B 203 29.200 51.193 −13.501 1.00 43.28 C ATOM 3570 C ALA B 203 28.297 51.802 −14.543 1.00 43.28 C ATOM 3571 O ALA B 203 27.899 51.127 −15.493 1.00 43.28 O ATOM 3572 CB ALA B 203 30.627 51.401 −13.905 1.00 43.28 C ATOM 3573 N GLY B 204 27.983 53.081 −14.374 1.00 43.96 N ATOM 3574 CA GLY B 204 27.246 53.799 −15.390 1.00 43.96 C ATOM 3575 C GLY B 204 28.036 53.728 −16.678 1.00 43.96 C ATOM 3576 O GLY B 204 28.618 52.693 −17.018 1.00 43.96 O ATOM 3577 N LEU B 205 28.085 54.833 −17.404 1.00 46.03 N ATOM 3578 CA LEU B 205 28.826 54.803 −18.647 1.00 46.03 C ATOM 3579 C LEU B 205 29.651 56.047 −18.936 1.00 46.03 C ATOM 3580 O LEU B 205 29.272 57.177 −18.601 1.00 46.03 O ATOM 3581 CB LEU B 205 27.911 54.476 −19.823 1.00 46.03 C ATOM 3582 CG LEU B 205 28.680 54.178 −21.110 1.00 46.03 C ATOM 3583 CD1 LEU B 205 29.853 53.224 −20.866 1.00 46.03 C ATOM 3584 CD2 LEU B 205 27.720 53.635 −22.139 1.00 46.03 C ATOM 3585 N LYS B 206 30.796 55.788 −19.563 1.00 54.20 N ATOM 3586 CA LYS B 206 31.748 56.802 −19.975 1.00 54.20 C ATOM 3587 C LYS B 206 31.082 57.723 −20.984 1.00 54.20 C ATOM 3588 O LYS B 206 29.942 57.494 −21.395 1.00 54.20 O ATOM 3589 CB LYS B 206 32.972 56.128 −20.604 1.00 54.20 C ATOM 3590 CG LYS B 206 33.658 55.064 −19.729 1.00 54.20 C ATOM 3591 CD LYS B 206 34.833 55.646 −18.930 1.00 54.20 C ATOM 3592 CE LYS B 206 35.795 54.568 −18.399 1.00 54.20 C ATOM 3593 NZ LYS B 206 35.556 54.158 −16.978 1.00 54.20 N ATOM 3594 N VAL B 207 31.793 58.765 −21.393 1.00 41.97 N ATOM 3595 CA VAL B 207 31.213 59.722 −22.321 1.00 41.97 C ATOM 3596 C VAL B 207 31.621 59.436 −23.771 1.00 41.97 C ATOM 3597 O VAL B 207 31.073 60.013 −24.706 1.00 41.97 O ATOM 3598 CB VAL B 207 31.532 61.173 −21.903 1.00 41.97 C ATOM 3599 CG1 VAL B 207 30.681 62.155 −22.691 1.00 41.97 C ATOM 3600 CG2 VAL B 207 31.274 61.348 −20.416 1.00 41.97 C ATOM 3601 N CYS B 208 32.563 58.520 −23.959 1.00 57.56 N ATOM 3602 CA CYS B 208 32.949 58.119 −25.309 1.00 57.56 C ATOM 3603 C CYS B 208 32.065 56.990 −25.849 1.00 57.56 C ATOM 3604 O CYS B 208 32.264 56.496 −26.962 1.00 57.56 O ATOM 3605 CB CYS B 208 34.423 57.711 −25.352 1.00 57.56 C ATOM 3606 SG CYS B 208 34.891 56.487 −24.123 1.00 57.56 S ATOM 3607 N PHE B 209 31.078 56.593 −25.060 1.00 40.31 N ATOM 3608 CA PHE B 209 30.232 55.482 −25.444 1.00 40.31 C ATOM 3609 C PHE B 209 28.776 55.912 −25.553 1.00 40.31 C ATOM 3610 O PHE B 209 28.039 55.413 −26.404 1.00 40.31 O ATOM 3611 CB PHE B 209 30.387 54.350 −24.438 1.00 40.31 C ATOM 3612 CG PHE B 209 30.041 53.003 −24.987 1.00 40.31 C ATOM 3613 CD1 PHE B 209 30.774 52.459 −26.023 1.00 40.31 C ATOM 3614 CD2 PHE B 209 28.994 52.275 −24.458 1.00 40.31 C ATOM 3615 CE1 PHE B 209 30.458 51.218 −26.522 1.00 40.31 C ATOM 3616 CE2 PHE B 209 28.677 51.034 −24.947 1.00 40.31 C ATOM 3617 CZ PHE B 209 29.408 50.502 −25.980 1.00 40.31 C ATOM 3618 N GLY B 210 28.363 56.833 −24.685 1.00 50.22 N ATOM 3619 CA GLY B 210 27.028 57.390 −24.756 1.00 50.22 C ATOM 3620 C GLY B 210 26.798 57.883 −26.168 1.00 50.22 C ATOM 3621 O GLY B 210 25.740 57.657 −26.758 1.00 50.22 O ATOM 3622 N ILE B 211 27.814 58.543 −26.715 1.00 49.82 N ATOM 3623 CA ILE B 211 27.793 59.027 −28.091 1.00 49.82 C ATOM 3624 C ILE B 211 27.562 57.909 −29.110 1.00 49.82 C ATOM 3625 O ILE B 211 26.703 58.033 −29.982 1.00 49.82 O ATOM 3626 CB ILE B 211 29.112 59.733 −28.438 1.00 49.82 C ATOM 3627 CG1 ILE B 211 29.316 60.943 −27.528 1.00 49.82 C ATOM 3628 CG2 ILE B 211 29.140 60.127 −29.907 1.00 49.82 C ATOM 3629 CD1 ILE B 211 30.757 61.380 −27.417 1.00 49.82 C ATOM 3630 N GLN B 212 28.329 56.825 −29.008 1.00 54.05 N ATOM 3631 CA GLN B 212 28.175 55.703 −29.934 1.00 54.05 C ATOM 3632 C GLN B 212 26.817 55.015 −29.772 1.00 54.05 C ATOM 3633 O GLN B 212 26.400 54.219 −30.617 1.00 54.05 O ATOM 3634 CB GLN B 212 29.326 54.712 −29.775 1.00 54.05 C ATOM 3635 CG GLN B 212 30.665 55.268 −30.237 1.00 54.05 C ATOM 3636 CD GLN B 212 30.727 55.476 −31.741 1.00 54.05 C ATOM 3637 OE1 GLN B 212 29.781 55.168 −32.464 1.00 54.05 O ATOM 3638 NE2 GLN B 212 31.850 55.998 −32.219 1.00 54.05 N ATOM 3639 N LEU B 213 26.137 55.338 −28.674 1.00 36.23 N ATOM 3640 CA LEU B 213 24.757 54.917 −28.461 1.00 36.23 C ATOM 3641 C LEU B 213 23.785 55.989 −28.947 1.00 36.23 C ATOM 3642 O LEU B 213 22.572 55.777 −28.988 1.00 36.23 O ATOM 3643 CB LEU B 213 24.506 54.586 −26.991 1.00 36.23 C ATOM 3644 CG LEU B 213 25.126 53.264 −26.543 1.00 36.23 C ATOM 3645 CD1 LEU B 213 24.428 52.732 −25.304 1.00 36.23 C ATOM 3646 CD2 LEU B 213 25.069 52.235 −27.660 1.00 36.23 C ATOM 3647 N LEU B 214 24.324 57.149 −29.303 1.00 27.82 N ATOM 3648 CA LEU B 214 23.542 58.139 −30.025 1.00 27.82 C ATOM 3649 C LEU B 214 23.753 57.902 −31.510 1.00 27.82 C ATOM 3650 O LEU B 214 22.872 58.163 −32.324 1.00 27.82 O ATOM 3651 CB LEU B 214 23.938 59.560 −29.630 1.00 27.82 C ATOM 3652 CG LEU B 214 23.402 59.994 −28.267 1.00 27.82 C ATOM 3653 CD1 LEU B 214 23.525 61.483 −28.093 1.00 27.82 C ATOM 3654 CD2 LEU B 214 21.958 59.583 −28.136 1.00 27.82 C ATOM 3655 N ASN B 215 24.929 57.391 −31.853 1.00 53.45 N ATOM 3656 CA ASN B 215 25.203 56.974 −33.215 1.00 53.45 C ATOM 3657 C ASN B 215 24.562 55.640 −33.476 1.00 53.45 C ATOM 3658 O ASN B 215 24.578 55.138 −34.594 1.00 53.45 O ATOM 3659 CB ASN B 215 26.699 56.869 −33.465 1.00 53.45 C ATOM 3660 CG ASN B 215 27.255 58.104 −34.123 1.00 53.45 C ATOM 3661 OD1 ASN B 215 26.912 59.226 −33.745 1.00 53.45 O ATOM 3662 ND2 ASN B 215 28.115 57.911 −35.123 1.00 53.45 N ATOM 3663 N ALA B 216 24.008 55.061 −32.422 1.00 38.63 N ATOM 3664 CA ALA B 216 23.338 53.783 −32.526 1.00 38.63 C ATOM 3665 C ALA B 216 21.899 54.001 −32.968 1.00 38.63 C ATOM 3666 O ALA B 216 21.442 53.443 −33.964 1.00 38.63 O ATOM 3667 CB ALA B 216 23.376 53.087 −31.195 1.00 38.63 C ATOM 3668 N VAL B 217 21.187 54.823 −32.210 1.00 40.78 N ATOM 3669 CA VAL B 217 19.798 55.126 −32.503 1.00 40.78 C ATOM 3670 C VAL B 217 19.649 55.708 −33.910 1.00 40.78 C ATOM 3671 O VAL B 217 18.906 55.183 −34.734 1.00 40.78 O ATOM 3672 CB VAL B 217 19.233 56.116 −31.465 1.00 40.78 C ATOM 3673 CG1 VAL B 217 17.717 56.145 −31.523 1.00 40.78 C ATOM 3674 CG2 VAL B 217 19.708 55.743 −30.070 1.00 40.78 C ATOM 3675 N SER B 218 20.368 56.792 −34.173 1.00 15.36 N ATOM 3676 CA SER B 218 20.319 57.482 −35.451 1.00 15.36 C ATOM 3677 C SER B 218 20.446 56.518 −36.604 1.00 15.36 C ATOM 3678 O SER B 218 19.642 56.546 −37.524 1.00 15.36 O ATOM 3679 CB SER B 218 21.485 58.441 −35.527 1.00 15.36 C ATOM 3680 OG SER B 218 22.673 57.726 −35.232 1.00 15.36 O ATOM 3681 N ARG B 219 21.478 55.681 −36.553 1.00 13.24 N ATOM 3682 CA ARG B 219 21.719 54.688 −37.596 1.00 13.24 C ATOM 3683 C ARG B 219 20.565 53.705 −37.735 1.00 13.24 C ATOM 3684 O ARG B 219 20.253 53.265 −38.843 1.00 13.24 O ATOM 3685 CB ARG B 219 23.006 53.913 −37.327 1.00 13.24 C ATOM 3686 CG ARG B 219 24.251 54.729 −37.500 1.00 13.24 C ATOM 3687 CD ARG B 219 25.488 53.940 −37.137 1.00 13.24 C ATOM 3688 NE ARG B 219 26.617 54.836 −36.934 1.00 13.24 N ATOM 3689 CZ ARG B 219 27.857 54.443 −36.678 1.00 13.24 C ATOM 3690 NH1 ARG B 219 28.150 53.154 −36.598 1.00 13.24 N ATOM 3691 NH2 ARG B 219 28.808 55.347 −36.510 1.00 13.24 N ATOM 3692 N VAL B 220 19.945 53.353 −36.611 1.00 37.77 N ATOM 3693 CA VAL B 220 18.797 52.452 −36.621 1.00 37.77 C ATOM 3694 C VAL B 220 17.559 53.141 −37.206 1.00 37.77 C ATOM 3695 O VAL B 220 16.779 52.532 −37.933 1.00 37.77 O ATOM 3696 CB VAL B 220 18.506 51.901 −35.211 1.00 37.77 C ATOM 3697 CG1 VAL B 220 17.330 50.940 −35.242 1.00 37.77 C ATOM 3698 CG2 VAL B 220 19.746 51.212 −34.662 1.00 37.77 C ATOM 3699 N GLU B 221 17.404 54.421 −36.905 1.00 17.15 N ATOM 3700 CA GLU B 221 16.298 55.207 −37.429 1.00 17.15 C ATOM 3701 C GLU B 221 16.336 55.320 −38.956 1.00 17.15 C ATOM 3702 O GLU B 221 15.301 55.428 −39.603 1.00 17.15 O ATOM 3703 CB GLU B 221 16.311 56.594 −36.790 1.00 17.15 C ATOM 3704 CG GLU B 221 15.198 57.513 −37.268 1.00 17.15 C ATOM 3705 CD GLU B 221 14.918 58.662 −36.305 1.00 17.15 C ATOM 3706 OE1 GLU B 221 15.352 59.802 −36.615 1.00 17.15 O ATOM 3707 OE2 GLU B 221 14.272 58.415 −35.249 1.00 17.15 O ATOM 3708 N ARG B 222 17.531 55.302 −39.530 1.00 47.13 N ATOM 3709 CA ARG B 222 17.664 55.311 −40.981 1.00 47.13 C ATOM 3710 C ARG B 222 17.492 53.900 −41.503 1.00 47.13 C ATOM 3711 O ARG B 222 17.218 53.694 −42.684 1.00 47.13 O ATOM 3712 CB ARG B 222 19.041 55.829 −41.411 1.00 47.13 C ATOM 3713 CG ARG B 222 19.266 57.320 −41.207 1.00 47.13 C ATOM 3714 CD ARG B 222 20.419 57.829 −42.052 1.00 47.13 C ATOM 3715 NE ARG B 222 21.615 56.998 −41.942 1.00 47.13 N ATOM 3716 CZ ARG B 222 22.506 57.091 −40.961 1.00 47.13 C ATOM 3717 NH1 ARG B 222 22.330 57.974 −39.986 1.00 47.13 N ATOM 3718 NH2 ARG B 222 23.570 56.296 −40.951 1.00 47.13 N ATOM 3719 N ALA B 223 17.659 52.932 −40.610 1.00 45.84 N ATOM 3720 CA ALA B 223 17.735 51.526 −40.995 1.00 45.84 C ATOM 3721 C ALA B 223 16.378 50.838 −41.125 1.00 45.84 C ATOM 3722 O ALA B 223 16.192 49.981 −41.980 1.00 45.84 O ATOM 3723 CB ALA B 223 18.624 50.765 −40.016 1.00 45.84 C ATOM 3724 N LEU B 224 15.433 51.216 −40.279 1.00 37.86 N ATOM 3725 CA LEU B 224 14.132 50.560 −40.249 1.00 37.86 C ATOM 3726 C LEU B 224 13.474 50.352 −41.607 1.00 37.86 C ATOM 3727 O LEU B 224 12.971 49.268 −41.873 1.00 37.86 O ATOM 3728 CB LEU B 224 13.183 51.326 −39.341 1.00 37.86 C ATOM 3729 CG LEU B 224 13.749 51.579 −37.946 1.00 37.86 C ATOM 3730 CD1 LEU B 224 13.018 52.738 −37.274 1.00 37.86 C ATOM 3731 CD2 LEU B 224 13.696 50.309 −37.100 1.00 37.86 C ATOM 3732 N PRO B 225 13.459 51.388 −42.465 1.00 45.91 N ATOM 3733 CA PRO B 225 12.687 51.303 −43.714 1.00 45.91 C ATOM 3734 C PRO B 225 13.214 50.234 −44.653 1.00 45.91 C ATOM 3735 O PRO B 225 12.463 49.636 −45.419 1.00 45.91 O ATOM 3736 CB PRO B 225 12.905 52.680 −44.355 1.00 45.91 C ATOM 3737 CG PRO B 225 13.332 53.568 −43.240 1.00 45.91 C ATOM 3738 CD PRO B 225 14.127 52.692 −42.329 1.00 45.91 C ATOM 3739 N LYS B 226 14.517 50.013 −44.589 1.00 45.72 N ATOM 3740 CA LYS B 226 15.176 49.094 −45.487 1.00 45.72 C ATOM 3741 C LYS B 226 15.128 47.693 −44.896 1.00 45.72 C ATOM 3742 O LYS B 226 15.836 46.792 −45.339 1.00 45.72 O ATOM 3743 CB LYS B 226 16.616 49.557 −45.719 1.00 45.72 C ATOM 3744 CG LYS B 226 16.720 51.065 −46.006 1.00 45.72 C ATOM 3745 CD LYS B 226 18.057 51.480 −46.622 1.00 45.72 C ATOM 3746 CE LYS B 226 17.863 52.638 −47.609 1.00 45.72 C ATOM 3747 NZ LYS B 226 19.139 53.315 −48.003 1.00 45.72 N ATOM 3748 N LEU B 227 14.274 47.511 −43.897 1.00 23.61 N ATOM 3749 CA LEU B 227 14.141 46.215 −43.242 1.00 23.61 C ATOM 3750 C LEU B 227 13.135 45.306 −43.930 1.00 23.61 C ATOM 3751 O LEU B 227 11.941 45.613 −44.003 1.00 23.61 O ATOM 3752 CB LEU B 227 13.741 46.391 −41.783 1.00 23.61 C ATOM 3753 CG LEU B 227 14.893 46.707 −40.843 1.00 23.61 C ATOM 3754 CD1 LEU B 227 14.367 46.816 −39.433 1.00 23.61 C ATOM 3755 CD2 LEU B 227 15.929 45.615 −40.948 1.00 23.61 C ATOM 3756 N THR B 228 13.629 44.170 −44.405 1.00 24.27 N ATOM 3757 CA THR B 228 12.813 43.224 −45.141 1.00 24.27 C ATOM 3758 C THR B 228 12.694 41.901 −44.385 1.00 24.27 C ATOM 3759 O THR B 228 11.806 41.082 −44.643 1.00 24.27 O ATOM 3760 CB THR B 228 13.449 42.954 −46.498 1.00 24.27 C ATOM 3761 OG1 THR B 228 14.614 42.135 −46.321 1.00 24.27 O ATOM 3762 CG2 THR B 228 13.846 44.267 −47.145 1.00 24.27 C ATOM 3763 N VAL B 229 13.601 41.712 −43.439 1.00 17.37 N ATOM 3764 CA VAL B 229 13.755 40.444 −42.752 1.00 17.37 C ATOM 3765 C VAL B 229 12.589 40.171 −41.811 1.00 17.37 C ATOM 3766 O VAL B 229 12.113 41.065 −41.122 1.00 17.37 O ATOM 3767 CB VAL B 229 15.097 40.425 −41.979 1.00 17.37 C ATOM 3768 CG1 VAL B 229 15.187 41.626 −41.040 1.00 17.37 C ATOM 3769 CG2 VAL B 229 15.289 39.111 −41.232 1.00 17.37 C ATOM 3770 N PRO B 230 12.118 38.923 −41.790 1.00 17.18 N ATOM 3771 CA PRO B 230 11.074 38.499 −40.855 1.00 17.18 C ATOM 3772 C PRO B 230 11.554 38.735 −39.450 1.00 17.18 C ATOM 3773 O PRO B 230 12.699 38.400 −39.176 1.00 17.18 O ATOM 3774 CB PRO B 230 11.000 36.982 −41.074 1.00 17.18 C ATOM 3775 CG PRO B 230 11.590 36.741 −42.402 1.00 17.18 C ATOM 3776 CD PRO B 230 12.611 37.813 −42.620 1.00 17.18 C ATOM 3777 N PHE B 231 10.723 39.283 −38.575 1.00 6.64 N ATOM 3778 CA PHE B 231 11.102 39.333 −37.167 1.00 6.64 C ATOM 3779 C PHE B 231 9.953 39.151 −36.202 1.00 6.64 C ATOM 3780 O PHE B 231 8.811 39.461 −36.529 1.00 6.64 O ATOM 3781 CB PHE B 231 11.822 40.624 −36.836 1.00 6.64 C ATOM 3782 CG PHE B 231 10.987 41.838 −37.004 1.00 6.64 C ATOM 3783 CD1 PHE B 231 10.348 42.401 −35.920 1.00 6.64 C ATOM 3784 CD2 PHE B 231 10.867 42.435 −38.244 1.00 6.64 C ATOM 3785 CE1 PHE B 231 9.597 43.539 −36.070 1.00 6.64 C ATOM 3786 CE2 PHE B 231 10.115 43.566 −38.407 1.00 6.64 C ATOM 3787 CZ PHE B 231 9.474 44.124 −37.318 1.00 6.64 C ATOM 3788 N LEU B 232 10.276 38.626 −35.020 1.00 7.61 N ATOM 3789 CA LEU B 232 9.340 38.534 −33.906 1.00 7.61 C ATOM 3790 C LEU B 232 9.840 39.516 −32.894 1.00 7.61 C ATOM 3791 O LEU B 232 11.035 39.595 −32.662 1.00 7.61 O ATOM 3792 CB LEU B 232 9.324 37.125 −33.296 1.00 7.61 C ATOM 3793 CG LEU B 232 8.986 36.954 −31.803 1.00 7.61 C ATOM 3794 CD1 LEU B 232 7.552 37.279 −31.497 1.00 7.61 C ATOM 3795 CD2 LEU B 232 9.296 35.546 −31.337 1.00 7.61 C ATOM 3796 N LEU B 233 8.938 40.266 −32.285 1.00 9.34 N ATOM 3797 CA LEU B 233 9.350 41.367 −31.429 1.00 9.34 C ATOM 3798 C LEU B 233 8.579 41.399 −30.123 1.00 9.34 C ATOM 3799 O LEU B 233 7.388 41.694 −30.112 1.00 9.34 O ATOM 3800 CB LEU B 233 9.161 42.690 −32.170 1.00 9.34 C ATOM 3801 CG LEU B 233 9.307 43.970 −31.364 1.00 9.34 C ATOM 3802 CD1 LEU B 233 10.726 44.129 −30.894 1.00 9.34 C ATOM 3803 CD2 LEU B 233 8.913 45.132 −32.231 1.00 9.34 C ATOM 3804 N LEU B 234 9.262 41.105 −29.022 1.00 16.65 N ATOM 3805 CA LEU B 234 8.655 41.150 −27.691 1.00 16.65 C ATOM 3806 C LEU B 234 9.123 42.397 −26.941 1.00 16.65 C ATOM 3807 O LEU B 234 10.268 42.808 −27.085 1.00 16.65 O ATOM 3808 CB LEU B 234 9.026 39.892 −26.912 1.00 16.65 C ATOM 3809 CG LEU B 234 8.969 38.575 −27.693 1.00 16.65 C ATOM 3810 CD1 LEU B 234 9.451 37.413 −26.846 1.00 16.65 C ATOM 3811 CD2 LEU B 234 7.571 38.316 −28.180 1.00 16.65 C ATOM 3812 N GLN B 235 8.248 42.996 −26.140 1.00 4.39 N ATOM 3813 CA GLN B 235 8.532 44.303 −25.548 1.00 4.39 C ATOM 3814 C GLN B 235 7.677 44.587 −24.321 1.00 4.39 C ATOM 3815 O GLN B 235 6.454 44.592 −24.408 1.00 4.39 O ATOM 3816 CB GLN B 235 8.290 45.393 −26.592 1.00 4.39 C ATOM 3817 CG GLN B 235 8.138 46.786 −26.037 1.00 4.39 C ATOM 3818 CD GLN B 235 9.460 47.379 −25.614 1.00 4.39 C ATOM 3819 OE1 GLN B 235 10.501 47.070 −26.196 1.00 4.39 O ATOM 3820 NE2 GLN B 235 9.433 48.235 −24.595 1.00 4.39 N ATOM 3821 N GLY B 236 8.312 44.832 −23.179 1.00 9.27 N ATOM 3822 CA GLY B 236 7.577 45.165 −21.970 1.00 9.27 C ATOM 3823 C GLY B 236 6.907 46.531 −21.989 1.00 9.27 C ATOM 3824 O GLY B 236 7.489 47.524 −22.409 1.00 9.27 O ATOM 3825 N SER B 237 5.667 46.584 −21.529 1.00 4.92 N ATOM 3826 CA SER B 237 4.950 47.849 −21.439 1.00 4.92 C ATOM 3827 C SER B 237 5.710 48.880 −20.609 1.00 4.92 C ATOM 3828 O SER B 237 5.782 50.051 −20.976 1.00 4.92 O ATOM 3829 CB SER B 237 3.555 47.632 −20.840 1.00 4.92 C ATOM 3830 OG SER B 237 3.052 48.827 −20.259 1.00 4.92 O ATOM 3831 N ALA B 238 6.277 48.429 −19.494 1.00 13.18 N ATOM 3832 CA ALA B 238 6.902 49.311 −18.514 1.00 13.18 C ATOM 3833 C ALA B 238 8.420 49.280 −18.588 1.00 13.18 C ATOM 3834 O ALA B 238 9.085 48.863 −17.643 1.00 13.18 O ATOM 3835 CB ALA B 238 6.444 48.930 −17.124 1.00 13.18 C ATOM 3836 N ASP B 239 8.960 49.751 −19.706 1.00 22.50 N ATOM 3837 CA ASP B 239 10.385 49.634 −19.998 1.00 22.50 C ATOM 3838 C ASP B 239 11.099 50.981 −19.870 1.00 22.50 C ATOM 3839 O ASP B 239 11.068 51.820 −20.780 1.00 22.50 O ATOM 3840 CB ASP B 239 10.569 49.053 −21.402 1.00 22.50 C ATOM 3841 CG ASP B 239 11.906 48.405 −21.593 1.00 22.50 C ATOM 3842 OD1 ASP B 239 12.818 48.689 −20.803 1.00 22.50 O ATOM 3843 OD2 ASP B 239 12.043 47.614 −22.541 1.00 22.50 O ATOM 3844 N ARG B 240 11.747 51.177 −18.729 1.00 42.22 N ATOM 3845 CA ARG B 240 12.422 52.433 −18.442 1.00 42.22 C ATOM 3846 C ARG B 240 13.740 52.550 −19.189 1.00 42.22 C ATOM 3847 O ARG B 240 14.446 53.542 −19.061 1.00 42.22 O ATOM 3848 CB ARG B 240 12.660 52.576 −16.939 1.00 42.22 C ATOM 3849 CG ARG B 240 11.398 52.488 −16.097 1.00 42.22 C ATOM 3850 CD ARG B 240 10.774 53.849 −15.896 1.00 42.22 C ATOM 3851 NE ARG B 240 11.762 54.802 −15.405 1.00 42.22 N ATOM 3852 CZ ARG B 240 11.504 56.073 −15.112 1.00 42.22 C ATOM 3853 NH1 ARG B 240 10.275 56.563 −15.252 1.00 42.22 N ATOM 3854 NH2 ARG B 240 12.481 56.855 −14.674 1.00 42.22 N ATOM 3855 N LEU B 241 14.084 51.535 −19.963 1.00 33.87 N ATOM 3856 CA LEU B 241 15.327 51.591 −20.714 1.00 33.87 C ATOM 3857 C LEU B 241 15.061 51.825 −22.184 1.00 33.87 C ATOM 3858 O LEU B 241 15.100 52.954 −22.659 1.00 33.87 O ATOM 3859 CB LEU B 241 16.150 50.321 −20.508 1.00 33.87 C ATOM 3860 CG LEU B 241 17.321 50.533 −19.549 1.00 33.87 C ATOM 3861 CD1 LEU B 241 17.045 51.740 −18.660 1.00 33.87 C ATOM 3862 CD2 LEU B 241 17.596 49.283 −18.726 1.00 33.87 C ATOM 3863 N CYS B 242 14.810 50.747 −22.910 1.00 15.99 N ATOM 3864 CA CYS B 242 14.358 50.875 −24.278 1.00 15.99 C ATOM 3865 C CYS B 242 12.898 51.265 −24.231 1.00 15.99 C ATOM 3866 O CYS B 242 12.061 50.499 −23.769 1.00 15.99 O ATOM 3867 CB CYS B 242 14.542 49.558 −25.015 1.00 15.99 C ATOM 3868 SG CYS B 242 16.244 49.036 −24.986 1.00 15.99 S ATOM 3869 N ASP B 243 12.602 52.476 −24.676 1.00 5.85 N ATOM 3870 CA ASP B 243 11.228 52.934 −24.752 1.00 5.85 C ATOM 3871 C ASP B 243 10.477 52.004 −25.690 1.00 5.85 C ATOM 3872 O ASP B 243 10.979 51.646 −26.750 1.00 5.85 O ATOM 3873 CB ASP B 243 11.179 54.368 −25.283 1.00 5.85 C ATOM 3874 CG ASP B 243 9.821 55.017 −25.097 1.00 5.85 C ATOM 3875 OD1 ASP B 243 9.641 56.155 −25.581 1.00 5.85 O ATOM 3876 OD2 ASP B 243 8.935 54.399 −24.473 1.00 5.85 O ATOM 3877 N SER B 244 9.275 51.610 −25.295 1.00 12.38 N ATOM 3878 CA SER B 244 8.461 50.734 −26.116 1.00 12.38 C ATOM 3879 C SER B 244 7.828 51.487 −27.275 1.00 12.38 C ATOM 3880 O SER B 244 7.302 50.879 −28.194 1.00 12.38 O ATOM 3881 CB SER B 244 7.381 50.061 −25.273 1.00 12.38 C ATOM 3882 OG SER B 244 6.283 50.920 −25.087 1.00 12.38 O ATOM 3883 N LYS B 245 7.866 52.812 −27.237 1.00 36.85 N ATOM 3884 CA LYS B 245 7.375 53.582 −28.373 1.00 36.85 C ATOM 3885 C LYS B 245 8.203 53.207 −29.596 1.00 36.85 C ATOM 3886 O LYS B 245 7.756 53.317 −30.739 1.00 36.85 O ATOM 3887 CB LYS B 245 7.467 55.086 −28.106 1.00 36.85 C ATOM 3888 CG LYS B 245 6.796 55.949 −29.176 1.00 36.85 C ATOM 3889 CD LYS B 245 6.911 57.435 −28.841 1.00 36.85 C ATOM 3890 CE LYS B 245 6.012 58.308 −29.730 1.00 36.85 C ATOM 3891 NZ LYS B 245 5.862 59.705 −29.197 1.00 36.85 N ATOM 3892 N GLY B 246 9.420 52.751 −29.336 1.00 30.16 N ATOM 3893 CA GLY B 246 10.333 52.386 −30.399 1.00 30.16 C ATOM 3894 C GLY B 246 9.908 51.104 −31.079 1.00 30.16 C ATOM 3895 O GLY B 246 10.077 50.950 −32.287 1.00 30.16 O ATOM 3896 N ALA B 247 9.356 50.185 −30.291 1.00 22.17 N ATOM 3897 CA ALA B 247 8.912 48.895 −30.796 1.00 22.17 C ATOM 3898 C ALA B 247 7.841 49.095 −31.850 1.00 22.17 C ATOM 3899 O ALA B 247 7.846 48.428 −32.876 1.00 22.17 O ATOM 3900 CB ALA B 247 8.382 48.041 −29.663 1.00 22.17 C ATOM 3901 N TYR B 248 6.928 50.027 −31.595 1.00 40.43 N ATOM 3902 CA TYR B 248 5.865 50.344 −32.543 1.00 40.43 C ATOM 3903 C TYR B 248 6.419 50.945 −33.831 1.00 40.43 C ATOM 3904 O TYR B 248 5.942 50.665 −34.929 1.00 40.43 O ATOM 3905 CB TYR B 248 4.861 51.298 −31.900 1.00 40.43 C ATOM 3906 CG TYR B 248 4.192 50.710 −30.677 1.00 40.43 C ATOM 3907 CD1 TYR B 248 3.217 49.725 −30.800 1.00 40.43 C ATOM 3908 CD2 TYR B 248 4.536 51.130 −29.398 1.00 40.43 C ATOM 3909 CE1 TYR B 248 2.601 49.176 −29.687 1.00 40.43 C ATOM 3910 CE2 TYR B 248 3.922 50.584 −28.278 1.00 40.43 C ATOM 3911 CZ TYR B 248 2.958 49.606 −28.432 1.00 40.43 C ATOM 3912 OH TYR B 248 2.345 49.060 −27.330 1.00 40.43 O ATOM 3913 N LEU B 249 7.437 51.776 −33.688 1.00 37.77 N ATOM 3914 CA LEU B 249 8.072 52.375 −34.842 1.00 37.77 C ATOM 3915 C LEU B 249 8.638 51.285 −35.735 1.00 37.77 C ATOM 3916 O LEU B 249 8.478 51.303 −36.951 1.00 37.77 O ATOM 3917 CB LEU B 249 9.198 53.281 −34.383 1.00 37.77 C ATOM 3918 CG LEU B 249 9.320 54.573 −35.165 1.00 37.77 C ATOM 3919 CD1 LEU B 249 8.264 55.544 −34.669 1.00 37.77 C ATOM 3920 CD2 LEU B 249 10.711 55.117 −34.966 1.00 37.77 C ATOM 3921 N LEU B 250 9.317 50.338 −35.111 1.00 29.80 N ATOM 3922 CA LEU B 250 9.898 49.218 −35.822 1.00 29.80 C ATOM 3923 C LEU B 250 8.833 48.440 −36.573 1.00 29.80 C ATOM 3924 O LEU B 250 9.047 48.045 −37.717 1.00 29.80 O ATOM 3925 CB LEU B 250 10.612 48.296 −34.837 1.00 29.80 C ATOM 3926 CG LEU B 250 11.298 47.054 −35.397 1.00 29.80 C ATOM 3927 CD1 LEU B 250 11.944 47.369 −36.729 1.00 29.80 C ATOM 3928 CD2 LEU B 250 12.320 46.548 −34.400 1.00 29.80 C ATOM 3929 N MET B 251 7.692 48.212 −35.932 1.00 4.00 N ATOM 3930 CA MET B 251 6.620 47.471 −36.577 1.00 4.00 C ATOM 3931 C MET B 251 6.137 48.227 −37.793 1.00 4.00 C ATOM 3932 O MET B 251 5.910 47.645 −38.847 1.00 4.00 O ATOM 3933 CB MET B 251 5.453 47.234 −35.624 1.00 4.00 C ATOM 3934 CG MET B 251 5.609 46.017 −34.739 1.00 4.00 C ATOM 3935 SD MET B 251 5.613 44.460 −35.629 1.00 4.00 S ATOM 3936 CE MET B 251 3.928 44.401 −36.193 1.00 4.00 C ATOM 3937 N GLU B 252 5.998 49.536 −37.637 1.00 40.94 N ATOM 3938 CA GLU B 252 5.438 50.388 −38.680 1.00 40.94 C ATOM 3939 C GLU B 252 6.369 50.675 −39.849 1.00 40.94 C ATOM 3940 O GLU B 252 5.950 50.621 −41.003 1.00 40.94 O ATOM 3941 CB GLU B 252 4.992 51.712 −38.079 1.00 40.94 C ATOM 3942 CG GLU B 252 4.883 52.814 −39.086 1.00 40.94 C ATOM 3943 CD GLU B 252 4.228 54.040 −38.502 1.00 40.94 C ATOM 3944 OE1 GLU B 252 4.774 55.157 −38.676 1.00 40.94 O ATOM 3945 OE2 GLU B 252 3.168 53.877 −37.857 1.00 40.94 O ATOM 3946 N LEU B 253 7.628 50.976 −39.549 1.00 20.33 N ATOM 3947 CA LEU B 253 8.537 51.506 −40.555 1.00 20.33 C ATOM 3948 C LEU B 253 9.325 50.443 −41.309 1.00 20.33 C ATOM 3949 O LEU B 253 9.951 50.737 −42.330 1.00 20.33 O ATOM 3950 CB LEU B 253 9.478 52.540 −39.934 1.00 20.33 C ATOM 3951 CG LEU B 253 8.838 53.791 −39.306 1.00 20.33 C ATOM 3952 CD1 LEU B 253 9.909 54.786 −38.875 1.00 20.33 C ATOM 3953 CD2 LEU B 253 7.834 54.465 −40.244 1.00 20.33 C ATOM 3954 N ALA B 254 9.280 49.209 −40.819 1.00 12.57 N ATOM 3955 CA ALA B 254 9.962 48.103 −41.478 1.00 12.57 C ATOM 3956 C ALA B 254 9.163 47.638 −42.665 1.00 12.57 C ATOM 3957 O ALA B 254 7.947 47.711 −42.649 1.00 12.57 O ATOM 3958 CB ALA B 254 10.150 46.966 −40.509 1.00 12.57 C ATOM 3959 N LYS B 255 9.838 47.141 −43.689 1.00 28.60 N ATOM 3960 CA LYS B 255 9.121 46.645 −44.859 1.00 28.60 C ATOM 3961 C LYS B 255 9.028 45.123 −44.892 1.00 28.60 C ATOM 3962 O LYS B 255 8.723 44.532 −45.926 1.00 28.60 O ATOM 3963 CB LYS B 255 9.739 47.182 −46.148 1.00 28.60 C ATOM 3964 CG LYS B 255 9.694 48.706 −46.257 1.00 28.60 C ATOM 3965 CD LYS B 255 8.384 49.265 −45.716 1.00 28.60 C ATOM 3966 CE LYS B 255 8.126 50.654 −46.250 1.00 28.60 C ATOM 3967 NZ LYS B 255 9.370 51.471 −46.211 1.00 28.60 N ATOM 3968 N SER B 256 9.278 44.505 −43.743 1.00 6.23 N ATOM 3969 CA SER B 256 9.224 43.059 −43.603 1.00 6.23 C ATOM 3970 C SER B 256 7.806 42.575 −43.753 1.00 6.23 C ATOM 3971 O SER B 256 6.894 43.129 −43.149 1.00 6.23 O ATOM 3972 CB SER B 256 9.759 42.640 −42.235 1.00 6.23 C ATOM 3973 OG SER B 256 11.138 42.930 −42.127 1.00 6.23 O ATOM 3974 N GLN B 257 7.628 41.531 −44.558 1.00 33.05 N ATOM 3975 CA GLN B 257 6.310 40.963 −44.812 1.00 33.05 C ATOM 3976 C GLN B 257 5.925 39.989 −43.706 1.00 33.05 C ATOM 3977 O GLN B 257 4.777 39.554 −43.622 1.00 33.05 O ATOM 3978 CB GLN B 257 6.263 40.269 −46.181 1.00 33.05 C ATOM 3979 CG GLN B 257 6.731 41.133 −47.376 1.00 33.05 C ATOM 3980 CD GLN B 257 5.614 41.955 −48.024 1.00 33.05 C ATOM 3981 OE1 GLN B 257 4.475 41.500 −48.128 1.00 33.05 O ATOM 3982 NE2 GLN B 257 5.947 43.165 −48.476 1.00 33.05 N ATOM 3983 N ASP B 258 6.891 39.651 −42.856 1.00 12.95 N ATOM 3984 CA ASP B 258 6.624 38.812 −41.689 1.00 12.95 C ATOM 3985 C ASP B 258 6.972 39.544 −40.410 1.00 12.95 C ATOM 3986 O ASP B 258 7.977 39.235 −39.783 1.00 12.95 O ATOM 3987 CB ASP B 258 7.423 37.504 −41.752 1.00 12.95 C ATOM 3988 CG ASP B 258 6.938 36.459 −40.734 1.00 12.95 C ATOM 3989 OD1 ASP B 258 6.212 36.823 −39.772 1.00 12.95 O ATOM 3990 OD2 ASP B 258 7.290 35.268 −40.906 1.00 12.95 O ATOM 3991 N LYS B 259 6.142 40.516 −40.034 1.00 10.77 N ATOM 3992 CA LYS B 259 6.289 41.237 −38.767 1.00 10.77 C ATOM 3993 C LYS B 259 5.397 40.615 −37.710 1.00 10.77 C ATOM 3994 O LYS B 259 4.361 40.029 −38.028 1.00 10.77 O ATOM 3995 CB LYS B 259 5.919 42.711 −38.921 1.00 10.77 C ATOM 3996 CG LYS B 259 6.476 43.371 −40.162 1.00 10.77 C ATOM 3997 CD LYS B 259 6.351 44.883 −40.057 1.00 10.77 C ATOM 3998 CE LYS B 259 6.240 45.550 −41.417 1.00 10.77 C ATOM 3999 NZ LYS B 259 5.680 46.927 −41.318 1.00 10.77 N ATOM 4000 N THR B 260 5.798 40.737 −36.452 1.00 19.93 N ATOM 4001 CA THR B 260 5.001 40.224 −35.349 1.00 19.93 C ATOM 4002 C THR B 260 5.437 40.891 −34.066 1.00 19.93 C ATOM 4003 O THR B 260 6.573 40.717 −33.646 1.00 19.93 O ATOM 4004 CB THR B 260 5.188 38.715 −35.172 1.00 19.93 C ATOM 4005 OG1 THR B 260 5.339 38.080 −36.450 1.00 19.93 O ATOM 4006 CG2 THR B 260 3.997 38.123 −34.448 1.00 19.93 C ATOM 4007 N LEU B 261 4.547 41.657 −33.446 1.00 5.75 N ATOM 4008 CA LEU B 261 4.885 42.368 −32.222 1.00 5.75 C ATOM 4009 C LEU B 261 4.015 41.933 −31.068 1.00 5.75 C ATOM 4010 O LEU B 261 2.795 41.912 −31.172 1.00 5.75 O ATOM 4011 CB LEU B 261 4.727 43.878 −32.413 1.00 5.75 C ATOM 4012 CG LEU B 261 4.290 44.726 −31.195 1.00 5.75 C ATOM 4013 CD1 LEU B 261 5.358 44.773 −30.115 1.00 5.75 C ATOM 4014 CD2 LEU B 261 3.937 46.139 −31.609 1.00 5.75 C ATOM 4015 N LYS B 262 4.640 41.606 −29.950 1.00 11.03 N ATOM 4016 CA LYS B 262 3.884 41.332 −28.738 1.00 11.03 C ATOM 4017 C LYS B 262 4.230 42.332 −27.614 1.00 11.03 C ATOM 4018 O LYS B 262 5.384 42.720 −27.441 1.00 11.03 O ATOM 4019 CB LYS B 262 4.071 39.873 −28.291 1.00 11.03 C ATOM 4020 CG LYS B 262 3.289 39.528 −27.038 1.00 11.03 C ATOM 4021 CD LYS B 262 3.046 38.046 −26.876 1.00 11.03 C ATOM 4022 CE LYS B 262 2.139 37.822 −25.683 1.00 11.03 C ATOM 4023 NZ LYS B 262 1.686 36.422 −25.556 1.00 11.03 N ATOM 4024 N ILE B 263 3.218 42.768 −26.874 1.00 7.44 N ATOM 4025 CA ILE B 263 3.434 43.565 −25.676 1.00 7.44 C ATOM 4026 C ILE B 263 3.069 42.759 −24.425 1.00 7.44 C ATOM 4027 O ILE B 263 2.113 41.976 −24.421 1.00 7.44 O ATOM 4028 CB ILE B 263 2.623 44.879 −25.714 1.00 7.44 C ATOM 4029 CG1 ILE B 263 3.008 45.715 −26.942 1.00 7.44 C ATOM 4030 CG2 ILE B 263 2.806 45.684 −24.429 1.00 7.44 C ATOM 4031 CD1 ILE B 263 4.430 46.224 −26.934 1.00 7.44 C ATOM 4032 N TYR B 264 3.860 42.943 −23.372 1.00 16.61 N ATOM 4033 CA TYR B 264 3.588 42.352 −22.065 1.00 16.61 C ATOM 4034 C TYR B 264 3.315 43.470 −21.075 1.00 16.61 C ATOM 4035 O TYR B 264 4.244 44.094 −20.571 1.00 16.61 O ATOM 4036 CB TYR B 264 4.793 41.555 −21.586 1.00 16.61 C ATOM 4037 CG TYR B 264 5.091 40.314 −22.396 1.00 16.61 C ATOM 4038 CD1 TYR B 264 4.560 39.089 −22.032 1.00 16.61 C ATOM 4039 CD2 TYR B 264 5.921 40.363 −23.509 1.00 16.61 C ATOM 4040 CE1 TYR B 264 4.834 37.951 −22.753 1.00 16.61 C ATOM 4041 CE2 TYR B 264 6.198 39.226 −24.242 1.00 16.61 C ATOM 4042 CZ TYR B 264 5.648 38.023 −23.856 1.00 16.61 C ATOM 4043 OH TYR B 264 5.920 36.880 −24.563 1.00 16.61 O ATOM 4044 N GLU B 265 2.039 43.724 −20.806 1.00 24.89 N ATOM 4045 CA GLU B 265 1.624 44.901 −20.042 1.00 24.89 C ATOM 4046 C GLU B 265 2.140 44.896 −18.614 1.00 24.89 C ATOM 4047 O GLU B 265 1.850 43.984 −17.842 1.00 24.89 O ATOM 4048 CB GLU B 265 0.099 45.028 −20.034 1.00 24.89 C ATOM 4049 CG GLU B 265 −0.424 46.237 −19.277 1.00 24.89 C ATOM 4050 CD GLU B 265 −0.319 47.526 −20.066 1.00 24.89 C ATOM 4051 OE1 GLU B 265 0.453 47.573 −21.050 1.00 24.89 O ATOM 4052 OE2 GLU B 265 −1.013 48.496 −19.696 1.00 24.89 O ATOM 4053 N GLY B 266 2.899 45.928 −18.270 1.00 5.53 N ATOM 4054 CA GLY B 266 3.447 46.078 −16.934 1.00 5.53 C ATOM 4055 C GLY B 266 4.867 45.556 −16.836 1.00 5.53 C ATOM 4056 O GLY B 266 5.617 45.906 −15.917 1.00 5.53 O ATOM 4057 N ALA B 267 5.227 44.709 −17.797 1.00 34.70 N ATOM 4058 CA ALA B 267 6.525 44.049 −17.823 1.00 34.70 C ATOM 4059 C ALA B 267 7.660 45.050 −17.933 1.00 34.70 C ATOM 4060 O ALA B 267 7.467 46.181 −18.363 1.00 34.70 O ATOM 4061 CB ALA B 267 6.590 43.044 −18.960 1.00 34.70 C ATOM 4062 N TYR B 268 8.847 44.618 −17.537 1.00 7.95 N ATOM 4063 CA TYR B 268 9.998 45.489 −17.489 1.00 7.95 C ATOM 4064 C TYR B 268 10.829 45.342 −18.747 1.00 7.95 C ATOM 4065 O TYR B 268 10.288 45.224 −19.841 1.00 7.95 O ATOM 4066 CB TYR B 268 10.828 45.186 −16.248 1.00 7.95 C ATOM 4067 CG TYR B 268 10.318 45.869 −15.001 1.00 7.95 C ATOM 4068 CD1 TYR B 268 8.956 46.059 −14.793 1.00 7.95 C ATOM 4069 CD2 TYR B 268 11.195 46.313 −14.026 1.00 7.95 C ATOM 4070 CE1 TYR B 268 8.486 46.681 −13.655 1.00 7.95 C ATOM 4071 CE2 TYR B 268 10.732 46.935 −12.884 1.00 7.95 C ATOM 4072 CZ TYR B 268 9.378 47.114 −12.701 1.00 7.95 C ATOM 4073 OH TYR B 268 8.927 47.735 −11.556 1.00 7.95 O ATOM 4074 N HIS B 269 12.146 45.354 −18.600 1.00 11.31 N ATOM 4075 CA HIS B 269 13.001 45.340 −19.767 1.00 11.31 C ATOM 4076 C HIS B 269 13.491 43.939 −20.140 1.00 11.31 C ATOM 4077 O HIS B 269 13.209 43.415 −21.219 1.00 11.31 O ATOM 4078 CB HIS B 269 14.190 46.260 −19.551 1.00 11.31 C ATOM 4079 CG HIS B 269 15.105 46.329 −20.731 1.00 11.31 C ATOM 4080 ND1 HIS B 269 14.756 46.968 −21.900 1.00 11.31 N ATOM 4081 CD2 HIS B 269 16.348 45.832 −20.928 1.00 11.31 C ATOM 4082 CE1 HIS B 269 15.749 46.873 −22.764 1.00 11.31 C ATOM 4083 NE2 HIS B 269 16.728 46.192 −22.198 1.00 11.31 N ATOM 4084 N VAL B 270 14.260 43.339 −19.255 1.00 14.28 N ATOM 4085 CA VAL B 270 14.744 42.023 −19.533 1.00 14.28 C ATOM 4086 C VAL B 270 13.539 41.118 −19.389 1.00 14.28 C ATOM 4087 O VAL B 270 13.264 40.606 −18.294 1.00 14.28 O ATOM 4088 CB VAL B 270 15.814 41.639 −18.539 1.00 14.28 C ATOM 4089 CG1 VAL B 270 16.686 40.535 −19.119 1.00 14.28 C ATOM 4090 CG2 VAL B 270 16.648 42.854 −18.205 1.00 14.28 C ATOM 4091 N LEU B 271 12.804 40.945 −20.487 1.00 6.51 N ATOM 4092 CA LEU B 271 11.594 40.132 −20.472 1.00 6.51 C ATOM 4093 C LEU B 271 11.890 38.641 −20.331 1.00 6.51 C ATOM 4094 O LEU B 271 11.039 37.879 −19.871 1.00 6.51 O ATOM 4095 CB LEU B 271 10.794 40.353 −21.740 1.00 6.51 C ATOM 4096 CG LEU B 271 10.611 41.781 −22.205 1.00 6.51 C ATOM 4097 CD1 LEU B 271 9.775 41.804 −23.471 1.00 6.51 C ATOM 4098 CD2 LEU B 271 9.928 42.543 −21.111 1.00 6.51 C ATOM 4099 N HIS B 272 13.090 38.225 −20.737 1.00 9.94 N ATOM 4100 CA HIS B 272 13.484 36.819 −20.644 1.00 9.94 C ATOM 4101 C HIS B 272 13.978 36.447 −19.244 1.00 9.94 C ATOM 4102 O HIS B 272 14.471 35.339 −19.008 1.00 9.94 O ATOM 4103 CB HIS B 272 14.534 36.474 −21.697 1.00 9.94 C ATOM 4104 CG HIS B 272 15.710 37.401 −21.709 1.00 9.94 C ATOM 4105 ND1 HIS B 272 15.593 38.748 −21.961 1.00 9.94 N ATOM 4106 CD2 HIS B 272 17.032 37.161 −21.538 1.00 9.94 C ATOM 4107 CE1 HIS B 272 16.790 39.303 −21.927 1.00 9.94 C ATOM 4108 NE2 HIS B 272 17.679 38.362 −21.670 1.00 9.94 N ATOM 4109 N LYS B 273 13.821 37.392 −18.326 1.00 18.76 N ATOM 4110 CA LYS B 273 14.134 37.179 −16.931 1.00 18.76 C ATOM 4111 C LYS B 273 13.188 38.030 −16.095 1.00 18.76 C ATOM 4112 O LYS B 273 13.620 38.778 −15.219 1.00 18.76 O ATOM 4113 CB LYS B 273 15.577 37.578 −16.664 1.00 18.76 C ATOM 4114 CG LYS B 273 16.545 37.081 −17.707 1.00 18.76 C ATOM 4115 CD LYS B 273 17.947 36.958 −17.160 1.00 18.76 C ATOM 4116 CE LYS B 273 18.811 36.211 −18.146 1.00 18.76 C ATOM 4117 NZ LYS B 273 20.209 36.203 −17.698 1.00 18.76 N ATOM 4118 N GLU B 274 11.894 37.931 −16.392 1.00 20.63 N ATOM 4119 CA GLU B 274 10.870 38.661 −15.643 1.00 20.63 C ATOM 4120 C GLU B 274 10.096 37.726 −14.743 1.00 20.63 C ATOM 4121 O GLU B 274 10.517 36.600 −14.490 1.00 20.63 O ATOM 4122 CB GLU B 274 9.898 39.372 −16.588 1.00 20.63 C ATOM 4123 CG GLU B 274 10.063 40.868 −16.645 1.00 20.63 C ATOM 4124 CD GLU B 274 9.259 41.572 −15.584 1.00 20.63 C ATOM 4125 OE1 GLU B 274 9.563 42.742 −15.301 1.00 20.63 O ATOM 4126 OE2 GLU B 274 8.324 40.963 −15.032 1.00 20.63 O ATOM 4127 N LEU B 275 8.958 38.198 −14.259 1.00 6.52 N ATOM 4128 CA LEU B 275 8.066 37.333 −13.526 1.00 6.52 C ATOM 4129 C LEU B 275 7.888 36.084 −14.382 1.00 6.52 C ATOM 4130 O LEU B 275 7.984 36.161 −15.612 1.00 6.52 O ATOM 4131 CB LEU B 275 6.736 38.032 −13.286 1.00 6.52 C ATOM 4132 CG LEU B 275 6.819 39.344 −12.514 1.00 6.52 C ATOM 4133 CD1 LEU B 275 5.421 39.791 −12.149 1.00 6.52 C ATOM 4134 CD2 LEU B 275 7.663 39.190 −11.267 1.00 6.52 C ATOM 4135 N PRO B 276 7.638 34.928 −13.742 1.00 7.31 N ATOM 4136 CA PRO B 276 7.670 33.656 −14.474 1.00 7.31 C ATOM 4137 C PRO B 276 6.666 33.621 −15.616 1.00 7.31 C ATOM 4138 O PRO B 276 7.047 33.342 −16.747 1.00 7.31 O ATOM 4139 CB PRO B 276 7.295 32.627 −13.409 1.00 7.31 C ATOM 4140 CG PRO B 276 7.571 33.294 −12.125 1.00 7.31 C ATOM 4141 CD PRO B 276 7.285 34.740 −12.328 1.00 7.31 C ATOM 4142 N GLU B 277 5.404 33.914 −15.327 1.00 31.42 N ATOM 4143 CA GLU B 277 4.362 33.843 −16.345 1.00 31.42 C ATOM 4144 C GLU B 277 4.787 34.569 −17.609 1.00 31.42 C ATOM 4145 O GLU B 277 4.463 34.153 −18.722 1.00 31.42 O ATOM 4146 CB GLU B 277 3.045 34.426 −15.831 1.00 31.42 C ATOM 4147 CG GLU B 277 3.076 35.920 −15.555 1.00 31.42 C ATOM 4148 CD GLU B 277 3.112 36.247 −14.070 1.00 31.42 C ATOM 4149 OE1 GLU B 277 2.330 37.126 −13.649 1.00 31.42 O ATOM 4150 OE2 GLU B 277 3.905 35.628 −13.324 1.00 31.42 O ATOM 4151 N VAL B 278 5.519 35.658 −17.424 1.00 22.85 N ATOM 4152 CA VAL B 278 6.002 36.450 −18.542 1.00 22.85 C ATOM 4153 C VAL B 278 7.121 35.727 −19.263 1.00 22.85 C ATOM 4154 O VAL B 278 6.970 35.311 −20.408 1.00 22.85 O ATOM 4155 CB VAL B 278 6.525 37.807 −18.078 1.00 22.85 C ATOM 4156 CG1 VAL B 278 7.344 38.455 −19.173 1.00 22.85 C ATOM 4157 CG2 VAL B 278 5.370 38.693 −17.663 1.00 22.85 C ATOM 4158 N THR B 279 8.249 35.574 −18.592 1.00 16.22 N ATOM 4159 CA THR B 279 9.384 34.943 −19.232 1.00 16.22 C ATOM 4160 C THR B 279 8.935 33.705 −20.005 1.00 16.22 C ATOM 4161 O THR B 279 9.366 33.484 −21.134 1.00 16.22 O ATOM 4162 CB THR B 279 10.472 34.590 −18.212 1.00 16.22 C ATOM 4163 OG1 THR B 279 10.774 35.752 −17.427 1.00 16.22 O ATOM 4164 CG2 THR B 279 11.739 34.112 −18.918 1.00 16.22 C ATOM 4165 N ASN B 280 8.053 32.914 −19.400 1.00 5.34 N ATOM 4166 CA ASN B 280 7.560 31.701 −20.038 1.00 5.34 C ATOM 4167 C ASN B 280 6.852 32.023 −21.342 1.00 5.34 C ATOM 4168 O ASN B 280 7.106 31.415 −22.381 1.00 5.34 O ATOM 4169 CB ASN B 280 6.626 30.939 −19.101 1.00 5.34 C ATOM 4170 CG ASN B 280 7.369 30.226 −17.993 1.00 5.34 C ATOM 4171 OD1 ASN B 280 8.544 29.878 −18.141 1.00 5.34 O ATOM 4172 ND2 ASN B 280 6.689 30.003 −16.870 1.00 5.34 N ATOM 4173 N SER B 281 5.948 32.982 −21.281 1.00 19.18 N ATOM 4174 CA SER B 281 5.326 33.471 −22.485 1.00 19.18 C ATOM 4175 C SER B 281 6.417 33.739 −23.497 1.00 19.18 C ATOM 4176 O SER B 281 6.312 33.349 −24.656 1.00 19.18 O ATOM 4177 CB SER B 281 4.579 34.763 −22.195 1.00 19.18 C ATOM 4178 OG SER B 281 4.275 35.447 −23.393 1.00 19.18 O ATOM 4179 N VAL B 282 7.473 34.401 −23.039 1.00 12.64 N ATOM 4180 CA VAL B 282 8.583 34.782 −23.901 1.00 12.64 C ATOM 4181 C VAL B 282 9.307 33.575 −24.493 1.00 12.64 C ATOM 4182 O VAL B 282 9.573 33.538 −25.690 1.00 12.64 O ATOM 4183 CB VAL B 282 9.582 35.664 −23.154 1.00 12.64 C ATOM 4184 CG1 VAL B 282 10.757 35.965 −24.030 1.00 12.64 C ATOM 4185 CG2 VAL B 282 8.920 36.948 −22.739 1.00 12.64 C ATOM 4186 N PHE B 283 9.616 32.587 −23.660 1.00 24.18 N ATOM 4187 CA PHE B 283 10.251 31.356 −24.131 1.00 24.18 C ATOM 4188 C PHE B 283 9.355 30.601 −25.107 1.00 24.18 C ATOM 4189 O PHE B 283 9.815 30.036 −26.103 1.00 24.18 O ATOM 4190 CB PHE B 283 10.606 30.452 −22.948 1.00 24.18 C ATOM 4191 CG PHE B 283 11.932 30.764 −22.328 1.00 24.18 C ATOM 4192 CD1 PHE B 283 12.196 32.033 −21.832 1.00 24.18 C ATOM 4193 CD2 PHE B 283 12.913 29.793 −22.237 1.00 24.18 C ATOM 4194 CE1 PHE B 283 13.424 32.335 −21.258 1.00 24.18 C ATOM 4195 CE2 PHE B 283 14.144 30.084 −21.664 1.00 24.18 C ATOM 4196 CZ PHE B 283 14.400 31.358 −21.170 1.00 24.18 C ATOM 4197 N HIS B 284 8.065 30.600 −24.810 1.00 13.49 N ATOM 4198 CA HIS B 284 7.110 29.913 −25.642 1.00 13.49 C ATOM 4199 C HIS B 284 7.008 30.520 −27.020 1.00 13.49 C ATOM 4200 O HIS B 284 7.120 29.819 −28.026 1.00 13.49 O ATOM 4201 CB HIS B 284 5.749 29.970 −25.000 1.00 13.49 C ATOM 4202 CG HIS B 284 4.717 29.168 −25.724 1.00 13.49 C ATOM 4203 ND1 HIS B 284 4.564 27.811 −25.535 1.00 13.49 N ATOM 4204 CD2 HIS B 284 3.783 29.531 −26.632 1.00 13.49 C ATOM 4205 CE1 HIS B 284 3.574 27.374 −26.291 1.00 13.49 C ATOM 4206 NE2 HIS B 284 3.083 28.398 −26.966 1.00 13.49 N ATOM 4207 N GLU B 285 6.787 31.832 −27.057 1.00 7.44 N ATOM 4208 CA GLU B 285 6.566 32.556 −28.309 1.00 7.44 C ATOM 4209 C GLU B 285 7.745 32.422 −29.251 1.00 7.44 C ATOM 4210 O GLU B 285 7.581 32.180 −30.450 1.00 7.44 O ATOM 4211 CB GLU B 285 6.292 34.034 −28.037 1.00 7.44 C ATOM 4212 CG GLU B 285 5.213 34.300 −26.999 1.00 7.44 C ATOM 4213 CD GLU B 285 3.822 33.845 −27.426 1.00 7.44 C ATOM 4214 OE1 GLU B 285 3.546 33.797 −28.644 1.00 7.44 O ATOM 4215 OE2 GLU B 285 3.004 33.537 −26.530 1.00 7.44 O ATOM 4216 N ILE B 286 8.937 32.593 −28.704 1.00 13.48 N ATOM 4217 CA ILE B 286 10.139 32.405 −29.487 1.00 13.48 C ATOM 4218 C ILE B 286 10.242 30.959 −29.971 1.00 13.48 C ATOM 4219 O ILE B 286 10.591 30.703 −31.127 1.00 13.48 O ATOM 4220 CB ILE B 286 11.381 32.701 −28.669 1.00 13.48 C ATOM 4221 CG1 ILE B 286 11.222 33.994 −27.891 1.00 13.48 C ATOM 4222 CG2 ILE B 286 12.581 32.788 −29.575 1.00 13.48 C ATOM 4223 CD1 ILE B 286 12.232 34.116 −26.786 1.00 13.48 C ATOM 4224 N ASN B 287 9.965 30.012 −29.078 1.00 16.26 N ATOM 4225 CA ASN B 287 10.008 28.618 −29.457 1.00 16.26 C ATOM 4226 C ASN B 287 9.289 28.463 −30.787 1.00 16.26 C ATOM 4227 O ASN B 287 9.846 27.946 −31.749 1.00 16.26 O ATOM 4228 CB ASN B 287 9.372 27.735 −28.377 1.00 16.26 C ATOM 4229 CG ASN B 287 9.456 26.243 −28.705 1.00 16.26 C ATOM 4230 OD1 ASN B 287 8.816 25.751 −29.638 1.00 16.26 O ATOM 4231 ND2 ASN B 287 10.240 25.516 −27.924 1.00 16.26 N ATOM 4232 N MET B 288 8.060 28.951 −30.856 1.00 49.22 N ATOM 4233 CA MET B 288 7.235 28.686 −32.020 1.00 49.22 C ATOM 4234 C MET B 288 7.570 29.546 −33.223 1.00 49.22 C ATOM 4235 O MET B 288 7.652 29.033 −34.332 1.00 49.22 O ATOM 4236 CB MET B 288 5.770 28.788 −31.647 1.00 49.22 C ATOM 4237 CG MET B 288 5.481 27.953 −30.427 1.00 49.22 C ATOM 4238 SD MET B 288 3.962 26.994 −30.563 1.00 49.22 S ATOM 4239 CE MET B 288 2.775 28.293 −30.217 1.00 49.22 C ATOM 4240 N TRP B 289 7.766 30.844 −33.013 1.00 5.59 N ATOM 4241 CA TRP B 289 8.200 31.713 −34.105 1.00 5.59 C ATOM 4242 C TRP B 289 9.285 30.990 −34.912 1.00 5.59 C ATOM 4243 O TRP B 289 9.194 30.850 −36.132 1.00 5.59 O ATOM 4244 CB TRP B 289 8.725 33.055 −33.572 1.00 5.59 C ATOM 4245 CG TRP B 289 8.760 34.135 −34.628 1.00 5.59 C ATOM 4246 CD1 TRP B 289 7.716 34.921 −35.037 1.00 5.59 C ATOM 4247 CD2 TRP B 289 9.889 34.535 −35.418 1.00 5.59 C ATOM 4248 NE1 TRP B 289 8.128 35.781 −36.026 1.00 5.59 N ATOM 4249 CE2 TRP B 289 9.458 35.562 −36.277 1.00 5.59 C ATOM 4250 CE3 TRP B 289 11.218 34.123 −35.484 1.00 5.59 C ATOM 4251 CZ2 TRP B 289 10.311 36.176 −37.183 1.00 5.59 C ATOM 4252 CZ3 TRP B 289 12.060 34.739 −36.387 1.00 5.59 C ATOM 4253 CH2 TRP B 289 11.604 35.749 −37.220 1.00 5.59 C ATOM 4254 N VAL B 290 10.295 30.504 −34.204 1.00 26.73 N ATOM 4255 CA VAL B 290 11.388 29.774 −34.823 1.00 26.73 C ATOM 4256 C VAL B 290 10.965 28.426 −35.400 1.00 26.73 C ATOM 4257 O VAL B 290 11.131 28.179 −36.593 1.00 26.73 O ATOM 4258 CB VAL B 290 12.497 29.514 −33.814 1.00 26.73 C ATOM 4259 CG1 VAL B 290 13.598 28.668 −34.451 1.00 26.73 C ATOM 4260 CG2 VAL B 290 13.027 30.837 −33.267 1.00 26.73 C ATOM 4261 N SER B 291 10.433 27.556 −34.541 1.00 24.16 N ATOM 4262 CA SER B 291 10.008 26.211 −34.931 1.00 24.16 C ATOM 4263 C SER B 291 9.233 26.207 −36.229 1.00 24.16 C ATOM 4264 O SER B 291 9.476 25.372 −37.096 1.00 24.16 O ATOM 4265 CB SER B 291 9.126 25.607 −33.850 1.00 24.16 C ATOM 4266 OG SER B 291 9.807 25.588 −32.617 1.00 24.16 O ATOM 4267 N GLN B 292 8.292 27.141 −36.343 1.00 66.30 N ATOM 4268 CA GLN B 292 7.427 27.254 −37.511 1.00 66.30 C ATOM 4269 C GLN B 292 8.188 27.761 −38.730 1.00 66.30 C ATOM 4270 O GLN B 292 7.860 27.417 −39.860 1.00 66.30 O ATOM 4271 CB GLN B 292 6.239 28.171 −37.215 1.00 66.30 C ATOM 4272 CG GLN B 292 5.474 27.812 −35.943 1.00 66.30 C ATOM 4273 CD GLN B 292 4.833 26.437 −36.005 1.00 66.30 C ATOM 4274 OE1 GLN B 292 4.345 26.017 −37.051 1.00 66.30 O ATOM 4275 NE2 GLN B 292 4.828 25.732 −34.878 1.00 66.30 N ATOM 4276 N ARG B 293 9.201 28.584 −38.511 1.00 8.54 N ATOM 4277 CA ARG B 293 10.091 28.941 −39.607 1.00 8.54 C ATOM 4278 C ARG B 293 11.187 27.897 −39.637 1.00 8.54 C ATOM 4279 O ARG B 293 12.343 28.174 −39.926 1.00 8.54 O ATOM 4280 CB ARG B 293 10.647 30.352 −39.435 1.00 8.54 C ATOM 4281 CG ARG B 293 9.611 31.420 −39.708 1.00 8.54 C ATOM 4282 CD ARG B 293 9.738 32.592 −38.770 1.00 8.54 C ATOM 4283 NE ARG B 293 8.604 33.505 −38.895 1.00 8.54 N ATOM 4284 CZ ARG B 293 7.436 33.365 −38.259 1.00 8.54 C ATOM 4285 NH1 ARG B 293 7.231 32.334 −37.443 1.00 8.54 N ATOM 4286 NH2 ARG B 293 6.467 34.264 −38.438 1.00 8.54 N ATOM 4287 N THR B 294 10.791 26.669 −39.350 1.00 25.06 N ATOM 4288 CA THR B 294 11.737 25.582 −39.194 1.00 25.06 C ATOM 4289 C THR B 294 11.048 24.223 −39.350 1.00 25.06 C ATOM 4290 O THR B 294 11.332 23.469 −40.284 1.00 25.06 O ATOM 4291 CB THR B 294 12.436 25.688 −37.818 1.00 25.06 C ATOM 4292 OG1 THR B 294 13.728 26.286 −37.984 1.00 25.06 O ATOM 4293 CG2 THR B 294 12.582 24.322 −37.170 1.00 25.06 C ATOM 4294 C01 IN1 I 1 24.718 27.584 2.707 1.00 13.13 C ATOM 4295 C02 IN1 I 1 24.788 26.119 2.838 1.00 13.13 C ATOM 4296 C03 IN1 I 1 25.880 25.278 2.710 1.00 13.13 C ATOM 4297 C04 IN1 I 1 25.531 23.907 2.901 1.00 13.13 C ATOM 4298 C05 IN1 I 1 24.183 23.745 3.172 1.00 13.13 C ATOM 4299 C06 IN1 I 1 23.484 22.445 3.431 1.00 13.13 C ATOM 4300 N07 IN1 I 1 22.348 22.130 2.594 1.00 13.13 N ATOM 4301 C08 IN1 I 1 21.611 21.031 3.198 1.00 13.13 C ATOM 4302 C09 IN1 I 1 21.849 19.769 2.308 1.00 13.13 C ATOM 4303 C10 IN1 I 1 22.768 20.262 1.175 1.00 13.13 C ATOM 4304 C11 IN1 I 1 22.572 21.802 1.174 1.00 13.13 C ATOM 4305 C12 IN1 I 1 21.376 22.020 0.221 1.00 13.13 C ATOM 4306 O13 IN1 I 1 20.749 21.026 −0.165 1.00 13.13 O ATOM 4307 N14 IN1 I 1 21.195 23.165 −0.523 1.00 13.13 N ATOM 4308 C15 IN1 I 1 21.846 24.386 −0.147 1.00 13.13 C ATOM 4309 C16 IN1 I 1 20.950 25.498 0.301 1.00 13.13 C ATOM 4310 C17 IN1 I 1 19.740 25.205 0.927 1.00 13.13 C ATOM 4311 C18 IN1 I 1 18.913 26.221 1.400 1.00 13.13 C ATOM 4312 C19 IN1 I 1 19.294 27.550 1.251 1.00 13.13 C ATOM 4313 C20 IN1 I 1 20.498 27.850 0.636 1.00 13.13 C ATOM 4314 C21 IN1 I 1 21.327 26.836 0.159 1.00 13.13 C ATOM 4315 C22 IN1 I 1 22.604 27.221 −0.473 1.00 13.13 C ATOM 4316 N23 IN1 I 1 22.307 18.600 3.013 1.00 13.13 N ATOM 4317 C24 IN1 I 1 21.623 17.373 3.092 1.00 13.13 C ATOM 4318 N25 IN1 I 1 22.394 16.544 3.842 1.00 13.13 N ATOM 4319 N26 IN1 I 1 23.463 17.261 4.182 1.00 13.13 N ATOM 4320 N27 IN1 I 1 23.442 18.450 3.720 1.00 13.13 N ATOM 4321 S28 IN1 I 1 23.408 25.239 3.188 1.00 13.13 S ATOM 4322 C01 IN1 I 2 23.378 53.189 −19.347 1.00 35.21 C ATOM 4323 C02 IN1 I 2 22.515 52.002 −19.403 1.00 35.21 C ATOM 4324 C03 IN1 I 2 21.156 51.908 −19.644 1.00 35.21 C ATOM 4325 C04 IN1 I 2 20.706 50.547 −19.603 1.00 35.21 C ATOM 4326 C05 IN1 I 2 21.734 49.654 −19.332 1.00 35.21 C ATOM 4327 C06 IN1 I 2 21.650 48.168 −19.184 1.00 35.21 C ATOM 4328 N07 IN1 I 2 21.055 47.534 −20.337 1.00 35.21 N ATOM 4329 C08 IN1 I 2 20.034 46.540 −20.057 1.00 35.21 C ATOM 4330 C09 IN1 I 2 20.551 45.194 −20.647 1.00 35.21 C ATOM 4331 C10 IN1 I 2 21.669 45.569 −21.647 1.00 35.21 C ATOM 4332 C11 IN1 I 2 21.903 47.088 −21.443 1.00 35.21 C ATOM 4333 C12 IN1 I 2 21.517 47.874 −22.698 1.00 35.21 C ATOM 4334 O13 IN1 I 2 20.952 47.363 −23.678 1.00 35.21 O ATOM 4335 N14 IN1 I 2 21.365 49.218 −22.496 1.00 35.21 N ATOM 4336 C15 IN1 I 2 20.672 50.016 −23.465 1.00 35.21 C ATOM 4337 C16 IN1 I 2 20.749 51.445 −23.056 1.00 35.21 C ATOM 4338 C17 IN1 I 2 22.025 52.004 −22.935 1.00 35.21 C ATOM 4339 C18 IN1 I 2 22.178 53.327 −22.528 1.00 35.21 C ATOM 4340 C19 IN1 I 2 21.055 54.103 −22.225 1.00 35.21 C ATOM 4341 C20 IN1 I 2 19.780 53.548 −22.328 1.00 35.21 C ATOM 4342 C21 IN1 I 2 19.614 52.217 −22.738 1.00 35.21 C ATOM 4343 C22 IN1 I 2 18.231 51.695 −22.827 1.00 35.21 C ATOM 4344 N23 IN1 I 2 20.910 44.291 −19.595 1.00 35.21 N ATOM 4345 C24 IN1 I 2 20.657 42.907 −19.571 1.00 35.21 C ATOM 4346 N25 IN1 I 2 21.133 42.460 −18.378 1.00 35.21 N ATOM 4347 N26 IN1 I 2 21.627 43.540 −17.760 1.00 35.21 N ATOM 4348 N27 IN1 I 2 21.511 44.615 −18.436 1.00 35.21 N ATOM 4349 S28 IN1 I 2 23.180 50.488 −19.136 1.00 35.21 S ATOM 4350 O HOH W 1 35.245 17.583 0.089 1.00 10.88 O ATOM 4351 O HOH W 2 11.181 48.603 −16.494 1.00 5.32 O ATOM 4352 O HOH W 3 31.719 57.246 −35.017 1.00 16.27 O ATOM 4353 O HOH W 4 31.433 16.520 −1.572 1.00 20.61 O ATOM 4354 O HOH W 11 29.398 21.331 −42.103 1.00 8.28 O ATOM 4355 O HOH W 12 16.242 21.889 −19.683 1.00 34.18 O ATOM 4356 O HOH W 13 16.036 −3.836 −20.533 1.00 8.57 O ATOM 4357 O HOH W 14 15.007 3.768 7.892 1.00 4.73 O ATOM 4358 O HOH W 15 7.779 17.455 −16.581 1.00 7.79 O ATOM 4359 O HOH W 16 35.099 1.777 −14.112 1.00 8.72 O ATOM 4360 O HOH W 17 9.430 39.929 −45.308 1.00 10.98 O ATOM 4361 O HOH W 18 16.500 60.207 −25.077 1.00 4.51 O ATOM 4362 O HOH W 19 14.994 31.096 −2.451 1.00 12.36 O ATOM 4363 O HOH W 20 23.633 22.497 −44.728 1.00 14.65 O ATOM 4364 O HOH W 21 25.025 60.646 −34.782 1.00 18.65 O ATOM 4365 O HOH W 22 7.433 35.986 −9.162 1.00 7.22 O ATOM 4366 O HOH W 23 50.375 31.972 −22.449 1.00 22.52 O ATOM 4367 O HOH W 24 10.945 22.916 −0.665 1.00 18.98 O ATOM 4368 O HOH W 25 20.053 45.972 −2.691 1.00 7.02 O ATOM 4369 O HOH W 26 5.095 25.580 −27.397 1.00 7.95 O ATOM 4370 O HOH W 27 11.391 32.830 0.051 1.00 20.05 O ATOM 4371 O HOH W 28 11.183 28.625 −18.977 1.00 22.32 O ATOM 4372 O HOH W 29 18.905 55.801 −45.707 1.00 13.22 O ATOM 4373 O HOH W 30 45.852 41.312 −28.487 1.00 5.04 O ATOM 4374 O HOH W 31 20.391 28.238 14.635 1.00 8.21 O ATOM 4375 O HOH W 32 39.687 27.950 −29.601 1.00 26.80 O ATOM 4376 O HOH W 33 6.307 14.854 12.310 1.00 11.55 O ATOM 4377 O HOH W 34 36.524 23.371 −10.838 1.00 25.88 O ATOM 4378 O HOH W 35 37.732 28.568 2.999 1.00 24.61 O ATOM 4379 O HOH W 36 25.119 17.635 17.947 1.00 21.49 O ATOM 4380 O HOH W 37 46.158 6.529 −12.246 1.00 23.77 O ATOM 4381 O HOH W 38 16.123 43.959 −44.294 1.00 6.09 O ATOM 4382 O HOH W 39 14.900 23.088 −24.015 1.00 32.78 O ATOM 4383 O HOH W 40 35.559 30.654 −19.199 1.00 10.97 O ATOM 4384 O HOH W 41 10.661 37.253 −8.062 1.00 30.82 O ATOM 4385 O HOH W 42 12.108 63.261 −20.135 1.00 22.06 O ATOM 4386 O HOH W 43 10.022 19.841 17.725 1.00 17.42 O ATOM 4387 O HOH W 44 −3.246 23.799 −9.497 1.00 4.71 O ATOM 4388 O HOH W 45 13.628 −2.465 0.572 1.00 15.73 O ATOM 4389 O HOH W 46 24.257 44.737 −49.036 1.00 34.40 O ATOM 4390 O HOH W 47 10.204 22.898 15.322 1.00 11.95 O ATOM 4391 O HOH W 48 39.791 18.721 −9.102 1.00 13.70 O ATOM 4392 O HOH W 49 2.625 −1.831 −10.832 1.00 4.87 O ATOM 4393 O HOH W 50 14.899 −12.091 −17.113 1.00 5.27 O ATOM 4394 O HOH W 51 44.838 13.336 −0.960 1.00 6.98 O ATOM 4395 O HOH W 52 26.791 50.121 −37.250 1.00 28.06 O ATOM 4396 O HOH W 53 1.177 12.082 −13.399 1.00 15.40 O ATOM 4397 O HOH W 54 12.091 10.584 18.511 1.00 17.95 O ATOM 4398 O HOH W 55 16.295 8.648 12.919 1.00 29.75 O ATOM 4399 O HOH W 56 32.165 45.267 −42.713 1.00 29.10 O ATOM 4400 O HOH W 57 27.382 −2.337 −19.541 1.00 17.25 O ATOM 4401 O HOH W 58 14.316 −8.238 −3.377 1.00 27.04 O ATOM 4402 O HOH W 59 31.591 28.117 −25.523 1.00 18.65 O ATOM 4403 O HOH W 60 0.455 27.889 −2.821 1.00 8.01 O ATOM 4404 O HOH W 61 24.825 49.510 −2.541 1.00 24.57 O ATOM 4405 O HOH W 62 2.931 44.065 −10.716 1.00 14.25 O ATOM 4406 O HOH W 63 28.015 28.085 12.885 1.00 16.20 O ATOM 4407 O HOH W 64 15.532 54.243 −33.828 1.00 16.37 O ATOM 4408 O HOH W 65 18.238 0.909 4.713 1.00 17.12 O ATOM 4409 O HOH W 66 20.990 16.894 −29.781 1.00 11.71 O ATOM 4410 O HOH W 67 0.677 1.577 −1.509 1.00 14.26 O ATOM 4411 O HOH W 68 16.490 33.735 −19.189 1.00 32.75 O ATOM 4412 O HOH W 69 40.952 15.579 −9.940 1.00 33.72 O ATOM 4413 O HOH W 70 6.994 8.247 −19.505 1.00 11.82 O ATOM 4414 O HOH W 71 3.763 36.153 −0.397 1.00 20.87 O ATOM 4415 O HOH W 72 31.840 26.502 −0.331 1.00 42.43 O ATOM 4416 O HOH W 73 40.352 19.546 −12.338 1.00 16.37 O ATOM 4417 O HOH W 74 29.109 29.004 15.278 1.00 12.96 O ATOM 4418 O HOH W 75 32.559 3.696 −1.743 1.00 5.28 O ATOM 4419 O HOH W 76 5.351 −6.631 2.183 1.00 5.63 O END

REFERENCES Patents

-   U.S. Pat. No. 4,906,122A. Coupling for molecular models -   U.S. Pat. No. 5,030,103A. Dynamic molecular model -   U.S. Pat. No. 5,200,910A. Method for modelling the electron density     of a crystal -   U.S. Pat. No. 5,365,456A. Method for modelling the electron density     of a crystal -   U.S. Pat. No. 5,583,973A. Molecular modeling method and system -   U.S. Pat. No. 5,612,894A. System and method for molecular modeling     utilizing a sensitivity factor -   U.S. Pat. No. 5,733,720A. Genetically engineered cell lines for     detecting infectious herpesvirus and methods therefor -   U.S. Pat. No. 5,763,263A. Method and apparatus for producing     position addressable combinatorial libraries -   U.S. Pat. No. 5,942,428A. Crystals of the tyrosine kinase domain of     non-insulin receptor tyrosine kinases -   U.S. Pat. No. 5,994,503A. Nucleotide and protein sequences of lats     genes and methods based thereon -   U.S. Pat. No. 5,998,593A. Fluorescent enzyme substrates -   U.S. Pat. No. 6,037,117A. Methods using the Staphylococcus aureus     glycyl tRNA synthetase crystalline structure -   U.S. Pat. No. 6,071,700A. Heterologous polypeptide production in the     absence of nonsense-mediated MRNA decay functions -   U.S. Pat. No. 6,075,014A Inhibitors of &bgr;-lactamases and uses     therefor -   U.S. Pat. No. 6,075,123A. Cyclin-C variants, and diagnostic and     therapeutic uses thereof -   U.S. Pat. No. 6,080,576A. Vectors for gene trapping and gene     activation -   U.S. Pat. No. 6,093,573A. Three-dimensional structure of     bactericidal/permeability-increasing protein (BPI) -   U.S. Pat. No. 6,172,262B1. Amphiphilic agents for membrane protein     solubilization

Other References

-   Adams, P. D., K. Gopal, et al. (2004). “Recent developments in the     PHENIX software for automated crystallographic structure     determination.” J Synchrotron Radiat 11(Pt 1): 53-5. -   Adams, P. D., R. W. Grosse-Kunstleve, et al. (2002). “PHENIX:     building new software for automated crystallographic structure     determination.” Acta Crystallogr D Biol Crystallogr 58(Pt 11):     1948-54. -   Altschul, S. F. (1993). “A protein alignment scoring system     sensitive at all evolutionary distances.” J. Mol. Evol. 36: 290-300. -   Altschul, S. F., M. S. Boguski, et al. (1994). “Issues in searching     molecular sequence databases.” Nature Genetics 6: 119-129. -   Altschul, S. F., W. Gish, et al. (1990). “Basic local alignment     search tool.” J Mol Biol 215(3): 403-10. -   Bacon, D. J. and J. Moult (1992). “Docking by Least-squares Fitting     of Molecular Surface Patterns.” J. Mol. Biol. 225: 849-858. -   Bartlett, P. A., G. T. Shea, et al. (1989). “CAVEAT: A Program to     Facilitate the Structure-Derived Design of Biologically Active     Molecules.”” In Molecular Recognition in Chemical and Biological     Problems, Special Pub., Royal Chem. Soc. 78: 82-196. -   Bohm, H.-J. (1992). “The Computer Program LUDI: A New Method for the     De Novo Design of Enzyme Inhibitors.” J. Computer-Aided Molecular     Design 6: 61-78. -   Boutselakis, H., D. Dimitropoulos, et al. (2003). “E-MSD: the     European Bioinformatics Institute Macromolecular Structure     Database.” Nucleic Acids Res 31(1): 458-62. -   Bradford, M. M. (1976). “A rapid and sensitive method for the     quantitation of microgram quantities of protein utilizing the     principle of protein-dye binding.” Anal Biochem 72: 248-54. -   Brady, L., A. M. Brzozowski, et al. (1990). “A serine protease triad     forms the catalytic centre of a triacylglycerol lipase.” Nature     343(6260): 767-70. -   Brunger, A. T. (1993). X-Flor Version 3.1: A system for X-ray     crystallography and NMR. New Haven, Conn., Yale Univ. Pr. -   Brzozowski, A. M., U. Derewenda, et al. (1991). “A model for     interfacial activation in lipases from the structure of a fungal     lipase-inhibitor complex.” Nature 351(6326): 491-4. -   Campbell (1984). Biological Spectroscopy. Menlo Park, Calif., The     Benjamin/Cummings Publishing Co., Inc. -   Cantor, C. R. and P. R. Schimmel (1980). Biophysical Chemistry, Part     II, “Techniques for the Study of Biological Structure and     Function”, W. H. Freeman & Co. -   Carriere, F., K. Thirstrup, et al. (1997). “Pancreatic lipase     structure-function relationships by domain exchange.” Biochemistry     36(1): 239-48. -   Chahinian, H., L. Nini, et al. (2002). “Distinction between     esterases and lipases: a kinetic study with vinyl esters and TAG.”     Lipids 37(7): 653-62. -   Cohen (Editor), N. C. (1996). Guidebook on Molecular Modeling in     Drug Design, Academic Press. -   Cohen, N., J. Blaney, et al. (1990). “Molecular Modeling Software     and Methods for Medicinal Chemistry.” J. Med. Chem. 33: 883-894. -   Crowther, J. R. (1995). ELISA: Theory and Practice (Methods in     Molecular Biology), Humana Press. -   Delano, W. L. (2002). The PyMOL Molecular Graphics System. Palo     Alto, Calif., USA. -   Devlin (Editor), J. P. (1998). In High Throughput Screening: The     Discovery of Bioactive Substances. New York, Marcel Dekker Inc. -   Dinh, T. P., T. F. Freund, et al. (2002). “A role for monoglyceride     lipase in 2-arachidonoylglycerol inactivation.” Chem Phys Lipids     121(1-2): 149-58. -   Dinh, T. P., S. Kathuria, et al. (2004). “RNA interference suggests     a primary role for monoacylglycerol lipase in the degradation of the     endocannabinoid 2-arachidonoylglycerol.” Mol Pharmacol 66(5):     1260-4. -   Drenth, J. (1999). Principles of Protein X-ray Crystallography     (Springer Advanced Texts in Chemistry). Berlin, Springer Verlag. -   Dugi, K. A., H. L. Dichek, et al. (1995). “Human hepatic and     lipoprotein lipase: the loop covering the catalytic site mediates     lipase substrate specificity.” J Biol Chem 270(43): 25396-401. -   Dugi, K. A., H. L. Dichek, et al. (1992). “Human lipoprotein lipase:     the loop covering the catalytic site is essential for interaction     with lipid substrates.” J Biol Chem 267(35): 25086-91. -   Emsley, P. and K. Cowtan (2004). “Coot: model-building tools for     molecular graphics.” Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt     1): 2126-32. -   Farquhar-Smith, W. P., M. Egertova, et al. (2000). “Cannabinoid     CB(1) receptor expression in rat spinal cord.” Mol Cell Neurosci     15(6): 510-21. -   Faustinella, F., L. C. Smith, et al. (1992). “Functional topology of     a surface loop shielding the catalytic center in lipoprotein     lipase.” Biochemistry 31(32): 7219-23. -   Frisch, M. J., G. W. Trucks, et al. (1992). “Gaussian 92, Revision     C.” Gaussian, Inc. -   Galiegue, S., S. Mary, et al. (1995). “Expression of central and     peripheral cannabinoid receptors in human immune tissues and     leukocyte subpopulations.” Eur J Biochem 232(1): 54-61. -   Gans, W., A. Amann, et al. (1996). Fundamental Principals of     Molecular Modeling, Plenum Pub. Corp. -   Gonsiorek, W., C. Lunn, et al. (2000). “Endocannabinoid     2-arachidonyl glycerol is a full agonist through human type 2     cannabinoid receptor: antagonism by anandamide.” Mol Pharmacol     57(5): 1045-50. -   Goodford, P. J. (1985). “A Computational Procedure for Determining     Energetically Favorable Binding Sites on Biologically Important     Macromolecules.” J. Med. Chem. 28: 849-857. -   Goodsell, D. S. and A. J. Olsen (1990). “Automated Docking of     Substrates to Proteins by Simulated Annealing.” Proteins: Structure.     Function, and Genetics 8: 195-202. -   Guindon, J., J. Desroches, et al. (2007). “The antinociceptive     effects of intraplantar injections of 2-arachidonoyl glycerol are     mediated by cannabinoid CB2 receptors.” Br J Pharmacol 150(6):     693-701. -   Hanus, L., A. Breuer, et al. (1999). “HU-308: a specific agonist for     CB(2), a peripheral cannabinoid receptor.” Proc Natl Acad Sci USA     96(25): 14228-33. -   Heikinheimo, P., A. Goldman, et al. (1999). “Of barn owls and     bankers: a lush variety of alpha/beta hydrolases.” Structure 7(6):     R141-6. -   Henikoff, J. G. (1992). “Amino acid substitution matrices from     protein blocks.” Proc. Natl. Acad. Sci. USA(89): 10915-10919. -   Higgins, D. G., J. D. Thompson, et al. (1996). “Using CLUSTAL for     multiple sequence alignments.” Methods Enzymol 266: 383-402. -   Hohmann, A. G. (2002). “Spinal and peripheral mechanisms of     cannabinoid antinociception: behavioral, neurophysiological and     neuroanatomical perspectives.” Chem Phys Lipids 121(1-2): 173-90. -   Hohmann, A. G., J. N. Farthing, et al. (2004). “Selective activation     of cannabinoid CB2 receptors suppresses hyperalgesia evoked by     intradermal capsaicin.” J Pharmacol Exp Ther 308(2): 446-53. -   Hohmann, A. G. and M. Herkenham (1999). “Cannabinoid receptors     undergo axonal flow in sensory nerves.” Neuroscience 92(4): 1171-5. -   Hohmann, A. G., R. L. Suplita, et al. (2005). “An endocannabinoid     mechanism for stress-induced analgesia.” Nature 435(7045): 1108-12. -   Holmquist, M. (2000). “Alpha/Beta-hydrolase fold enzymes:     structures, functions and mechanisms.” Curr Protein Pept Sci 1(2):     209-35. -   Ibrahim, M. M., M. L. Rude, et al. (2006). “CB2 cannabinoid receptor     mediation of antinociception.” Pain 122(1-2): 36-42. -   Ishikawa, E. (1999). Ultrasensitive and rapid enzyme immunoassay,     In: Laboratory Techniques in Biochemistry and Molecular Biology.     Amsterdam, Elsevier. -   Kaneko, T., N. Tanaka, et al. (2005). “Crystal structures of RsbQ, a     stress-response regulator in Bacillus subtilis.” Protein Sci 14(2):     558-65. -   Karlin, S. and S. F. Altschul (1990). “Methods for assessing the     statistical significance of molecular sequence features by using     general scoring schemes.” Proc. Natl. Acad. Sci. USA 87: 2264-2268. -   Karlsson, M., J. A. Contreras, et al. (1997). “cDNA cloning, tissue     distribution, and identification of the catalytic triad of     monoglyceride lipase. Evolutionary relationship to esterases,     lysophospholipases, and haloperoxidases.” J Biol Chem 272(43):     27218-23. -   Karlsson, M., K. Reue, et al. (2001). “Exon-intron organization and     chromosomal localization of the mouse monoglyceride lipase gene.”     Gene 272(1-2): 11-8. -   Karlsson, M., H. Tornqvist, et al. (2000). “Expression,     purification, and characterization of histidine-tagged mouse     monoglyceride lipase from baculovirus-infected insect cells.”     Protein Expr Purif 18(3): 286-92. -   Kemeny (Editor), D. M. and S. J. Challacombe (Editor) (1988). Elisa     and Other Solid Phase Immunoassays: Theoretical and Practical     Aspects, New York, John Wiley and Sons. -   Kemeny, D. M. (1991). A Practical Guide to ELISA, Pergamon Press. -   Kuntz, I. D., J. M. Blaney, et al. (1982). “A geometric approach to     macromolecule-ligand interactions.” J Mol Biol 161(2): 269-88. -   Lee, C. and K. Irizarry (2001). “The GeneMine system for     genome/proteome annotation and collaborative data-mining.” IBM     Systems Journal 40(2). -   Levitt, M. (1992). “Accurate modeling of protein conformation by     automatic segment matching.” J Mol Biol 226(2): 507-33. -   Lipinski, C., F. Lombardo, et al. (1997). “Experimental and     computational approaches to estimate solubility and permeability in     drug discovery and development settings” Advanced Drug Delivery     Reviews 23(1-3): 3-25. -   Longenecker, K. L., S. M. Garrard, et al. (2001). “Protein     crystallization by rational mutagenesis of surface residues: Lys to     Ala mutations promote crystallization of RhoGDI.” Acta Crystallogr D     Biol Crystallogr 57(Pt 5): 679-88. -   Makara, J. K., M. Mor, et al. (2005). “Selective inhibition of 2-AG     hydrolysis enhances endocannabinoid signaling in hippocampus.” Nat     Neurosci 8(9): 1139-41. -   Malan, T. P., Jr., M. M. Ibrahim, et al. (2001). “CB2 cannabinoid     receptor-mediated peripheral antinociception.” Pain 93(3): 239-45. -   Malan, T. P., Jr., M. M. Ibrahim, et al. (2002). “Inhibition of pain     responses by activation of CB(2) cannabinoid receptors.” Chem Phys     Lipids 121(1-2): 191-200. -   Maresz, K., E. J. Carrier, et al. (2005). “Modulation of the     cannabinoid CB2 receptor in microglial cells in response to     inflammatory stimuli.” J Neurochem 95(2): 437-45. -   Martin, Y. C. (1992). “3D Database Searching in Drug Design.” J.     Med. Chem. 35: 2145-2154. -   Mary Ann Liebert (Publishers), I. (1995). The BIOTECHNOLOGY SOFTWARE     DIRECTORY, A Buyer's Guide. Larchmont, N.Y. Mary Ann Liebert, Inc.,     Publishers. -   Mateja, A., Y. Devedjiev, et al. (2002). “The impact of Glu→Ala and     Glu→Asp mutations on the crystallization properties of RhoGDI: the     structure of RhoGDI at 1.3 A resolution.” Acta Crystallogr D Biol     Crystallogr 58(Pt 12): 1983-91. -   Matsuda, L. A., S. J. Lolait, et al. (1990). “Structure of a     cannabinoid receptor and functional expression of the cloned cDNA.”     Nature 346(6284): 561-4. -   Matteucci and J. Caruthers (1981). J. Am. Chem. Soc. 103(3):     185-3191. -   Mccoy, A. J., R. W. Grosse-Kunstleve, et al. (2007). “Phaser     crystallographic software.” Journal of Applied Crystallography     40(4): 658-674. -   Meng, E. C., B. K. Shoichet, et al. (1992). “Automated docking with     grid-based energy evaluation.” J. Comp. Chem. 13: 505-524. -   Miranker, A. and M. Karplus (1991). “Functionality Maps of Binding     Sites: A Multiple Copy Simultaneous Search Method.” Proteins:     Structure, Function and Genetics 11: 29-34. -   Munro, S., K. L. Thomas, et al. (1993). “Molecular characterization     of a peripheral receptor for cannabinoids.” Nature 365(6441): 61-5. -   Navia, M. A. and M. A. Murcko (1992). “The Use of Structural     Information in Drug Design.” Current Opinions in Structural Biology     2: 202-210 -   Nini, L., L. Sarda, et al. (2001). “Lipase-catalysed hydrolysis of     short-chain substrates in solution and in emulsion: a kinetic     study.” Biochim Biophys Acta 1534(1): 34-44. -   Nishibata, Y. and A. Itai (1991). “Automatic creation of drug     candidate structures based on receptor structure. Starting point for     artificial lead generation.” Tetrahedron 47: 8985-8990. -   Norton, P. A. and J. M. Coffin (1985). “Bacterial beta-galactosidase     as a marker of Rous sarcoma virus gene expression and replication.”     Mol Cell Biol 5(2): 281-90. -   Ollis, D. L., E. Cheah, et al. (1992). “The alpha/beta hydrolase     fold.” Protein Eng 5(3): 197-211. -   Otwinowski, Z. and W. Minor (1997). Processing of X-ray Diffraction     Data Collected in Oscillation Mode. Methods in Enzymology. C. W.     Carter and R. M. Sweet. New York, Academic Press. 276: 307-326. -   Pantoliano, M. W., E. C. Petrella, et al. (2001). “High-density     miniaturized thermal shift assays as a general strategy for drug     discovery.” J Biomol Screen 6(6): 429-40. -   Quartilho, A., H. P. Mata, et al. (2003). “Inhibition of     inflammatory hyperalgesia by activation of peripheral CB2     cannabinoid receptors.” Anesthesiology 99(4): 955-60. -   Rice, A. S., W. P. Farquhar-Smith, et al. (2002). “Endocannabinoids     and pain: spinal and peripheral analgesia in inflammation and     neuropathy.” Prostaglandins Leukot Essent Fatty Acids 66(2-3):     243-56. -   Richardson, J. D. (2000). “Cannabinoids modulate pain by multiple     mechanisms of actions.” The Journal of Pain 1(1): 2-14. -   Richardson, J. D., S. Kilo, et al. (1998). “Cannabinoids reduce     hyperalgesia and inflammation via interaction with peripheral CB1     receptors.” Pain 75(1): 111-9. -   Rossmann, M. G. (1972). The molecular replacement method; a     collection of papers on the use of non-crystallographic symmetry.,     Gordon & Breach, New York. -   Rotstein, S. H. and M. A. Murcko (1993). “GroupBuild: a     fragment-based method for de novo drug design.” J Med Chem 36(12):     1700-10. -   Roussel, A., S. Canaan, et al. (1999). “Crystal structure of human     gastric lipase and model of lysosomal acid lipase, two lipolytic     enzymes of medical interest.” J Biol Chem 274(24): 16995-7002. -   Roussel, A., N. Miled, et al. (2002). “Crystal structure of the open     form of dog gastric lipase in complex with a phosphonate inhibitor.”     J Biol Chem 277(3): 2266-74. -   Saario, S. M., A. Poso, et al. (2006). “Fatty acid amide hydrolase     inhibitors from virtual screening of the endocannabinoid system.” J     Med Chem 49(15): 4650-6. -   Saario, S. M., O. M. Salo, et al. (2005). “Characterization of the     sulfhydryl-sensitive site in the enzyme responsible for hydrolysis     of 2-arachidonoyl-glycerol in rat cerebellar membranes.” Chem Biol     12(6): 649-56. -   Saario, S. M., J. R. Savinainen, et al. (2004). “Monoglyceride     lipase-like enzymatic activity is responsible for hydrolysis of     2-arachidonoylglycerol in rat cerebellar membranes.” Biochem     Pharmacol 67(7): 1381-7. -   Sambrook, J., E. F. Fritsch, et al. (1989). Molecular cloning. 2nd     ed., New York: Cold Spring Harbor Laboratory Press. -   Schlecht, M. (1998). Molecular Modeling on the PC, John Wiley &     Sons. -   Schrag, J. D., Y. G. Li, et al. (1991). “Ser-His-Glu triad forms the     catalytic site of the lipase from Geotrichum candidum.” Nature     351(6329): 761-4. -   Segel, I. H. (1975). Enzyme Kinetics: Behavior and Analysis of Rapid     Equilibrium and Steady-State Enzyme Systems, J. Wiley & Sons. -   Smith, W. B. (1996). Introduction to Theoretical Organic. Chemistry     and Molecular Modeling. New York, VCH Publishers. -   Somma-Delpero, C., A. Valette, et al. (1995). “Purification and     properties of a monoacylglycerol lipase in human erythrocytes.”     Biochem J 312 (Pt 2): 519-25. -   Sugiura, T., S. Kondo, et al. (2000). “Evidence that     2-arachidonoylglycerol but not N-palmitoylethanolamine or anandamide     is the physiological ligand for the cannabinoid CB2 receptor.     Comparison of the agonistic activities of various cannabinoid     receptor ligands in HL-60 cells.” J Biol Chem 275(1): 605-12. -   Sussman, J. L., D. Lin, et al. (1998). “Protein Data Bank (PDB):     database of three-dimensional structural information of biological     macromolecules.” Acta Crystallogr D Biol Crystallogr 54(Pt 6 Pt 1):     1078-84. -   Tatusova, T. A. and T. L. Madden (1999). “BLAST 2 Sequences, a new     tool for comparing protein and nucleotide sequences.” FEMS Microbiol     Lett 174(2): 247-50. -   Terwilliger, T. C., R. W. Grosse-Kunstleve, et al. (2008).     “Iterative model building, structure refinement and density     modification with the PHENIX AutoBuild wizard.” Acta Crystallogr D     Biol Crystallogr 64(Pt 1): 61-9. -   Thompson, J. D., D. G. Higgins, et al. (1994). “CLUSTAL W: improving     the sensitivity of progressive multiple sequence alignment through     sequence weighting, position-specific gap penalties and weight     matrix choice.” Nucleic Acids Res 22(22): 4673-80. -   Tornqvist, H. and P. Belfrage (1976). “Purification and some     properties of a monoacylglycerol-hydrolyzing enzyme of rat adipose     tissue.” J Biol Chem 251(3): 813-9. -   Travis, J. (1993). “Proteins and Organic Solvents Make an     Eye-Opening Mix.” Science 262: 1374 -   Tsirelson, V. G. and R. P. Ozerov (1996). Electron Density and     Bonding in Crystals: Principles, Theory and X-ray Diffraction     Experiments in Solid State Physics and Chemistry, Inst. of Physics     Pub. -   Van Den Berg, B., M. Tessari, et al. (1995). “NMR structures of     phospholipase A2 reveal conformational changes during interfacial     activation.” Nat Struct Biol 2(5): 402-6. -   Van Den Berg, B., M. Tessari, et al. (1995). “Solution structure of     porcine pancreatic phospholipase A2 complexed with micelles and a     competitive inhibitor.” J Biomol NMR 5(2): 110-21. -   Van Tilbeurgh, H., L. Sarda, et al. (1992). “Structure of the     pancreatic lipase-procolipase complex.” Nature 359(6391): 159-62. -   Vandevoorde, S. and D. M. Lambert (2005). “Focus on the three key     enzymes hydrolysing endocannabinoids as new drug targets.” Curr     Pharm Des 11(20): 2647-68. -   Walczak, J. S., V. Pichette, et al. (2005). “Behavioral,     pharmacological and molecular characterization of the saphenous     nerve partial ligation: a new model of neuropathic pain.”     Neuroscience 132(4): 1093-102. -   Wall, E. M., J. Cao, et al. (1997). “A novel poxvirus gene and its     human homolog are similar to an E. coli lysophospholipase.” Virus     Res 52(2): 157-67. -   Wang, X., C. S. Wang, et al. (1997). “The crystal structure of     bovine bile salt activated lipase: insights into the bile salt     activation mechanism.” Structure 5(9): 1209-18. -   Winkler, F. K., A. D'arcy, et al. (1990). “Structure of human     pancreatic lipase.” Nature 343(6260): 771-4. -   Woolfson, M. M. (1997). An Introduction to X-ray Crystallography.     Cambridge, UK, Cambridge Univ. Pr. 

1. A crystal of a monoacylglycerol lipase (MGLL) polypeptide in complex with a ligand, wherein the crystal has space group C2 and unit cell dimensions of a=128.6 Å, b=72.0 Å, and c=65.2 Å; wherein the MGLL polypeptide consists of the amino acid sequence of SEQ ID NO:7, and wherein the ligand has the formula: 